|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-1270 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 593.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 55 LAAIIHGTLLPLLMLVFGnmtdsftkaeasilpsitnqsgpnstLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIqvSL 134
Cdd:PTZ00265 67 VCATISGGTLPFFVSVFG--------------------------VIMKNMNLGENVNDIIFSLVLIGIFQFILSFI--SS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 135 WCL--AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWK 212
Cdd:PTZ00265 119 FCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNAR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 213 LTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAI 292
Cdd:PTZ00265 199 LTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 293 TASISIGIAYLLVYASYALAFWYGTSLVLS--------NEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:PTZ00265 279 MESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 365 FKIIDNEPSIDSFSTKGYKPDsiMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD 444
Cdd:PTZ00265 359 YEIINRKPLVENNDDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 445 PLEGVVSI-DGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG--------------RED---------------- 493
Cdd:PTZ00265 437 PTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDgndsqenknkrnscra 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 494 ------------VTMDEIEKAVKEANA---------------YDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVR 546
Cdd:PTZ00265 517 kcagdlndmsntTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 547 NPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVI--------------------------- 597
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnke 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 598 --------------------AGFDGGVIVEQGNHDELMREK-GIYFKLVMTQT--------------------------R 630
Cdd:PTZ00265 677 nnnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvsskkssnndndkdsdmkssaykdseR 756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 631 GNEIEP--GNNAYGSQS----------DTDASElTSEESKSPLIRRSIYRSvhRKQDQERRLSMKE--AVDEDVPLVSFw 696
Cdd:PTZ00265 757 GYDPDEmnGNSKHENESasnkksckmsDENASE-NNAGGKLPFLRNLFKRK--PKAPNNLRIVYREifSYKKDVTIIAL- 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 697 rilnlnlsewpyllvgvlCAVINGCIQPVFAIVFSRIVGVFSrddDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFG 776
Cdd:PTZ00265 833 ------------------SILVAGGLYPVFALLYAKYVSTLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNN 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 777 KAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYgwqlt 856
Cdd:PTZ00265 892 VIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYF----- 966
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 857 lllvviIPLI--VLGGI--IEMKLLSGQAL----KD--KKQLEISGKI----------------ATEAIENFRTIVSLTR 910
Cdd:PTZ00265 967 ------CPIVaaVLTGTyfIFMRVFAIRARltanKDveKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGL 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 911 EQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTS 990
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 991 SFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLK---PTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALV 1067
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1068 GSSGCGKSTVVQLLERFYD------------------------------------------------------PMAGSVF 1093
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKIL 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1094 LDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQ 1173
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1358
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIENGK- 1248
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDr 1436
|
1450 1460
....*....|....*....|....*..
gi 126927 1249 ----VKEHGTHQQLL-AQKGIYFSMVQ 1270
Cdd:PTZ00265 1437 tgsfVQAHGTHEELLsVQDGVYKKYVK 1463
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
38-631 |
7.14e-180 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 542.83 E-value: 7.14e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 38 MFRYAdWLDKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTkaeasilpsitnqSGPNSTLIISnssleeemaiYAYYY 117
Cdd:COG1132 12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-------------AGGDLSALLL----------LLLLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 118 TGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSIT 197
Cdd:COG1132 68 LGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 198 TFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYN 277
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 278 KNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANA 357
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 358 RGAAFEIFKIIDNEPSIDSfSTKGYKPDSIMGNLEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQ 437
Cdd:COG1132 308 LASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 438 LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPH 517
Cdd:COG1132 385 LLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 518 QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:COG1132 465 GYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRI 544
|
570 580 590
....*....|....*....|....*....|....
gi 126927 598 AGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRG 631
Cdd:COG1132 545 LVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
694-1271 |
4.72e-167 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 509.32 E-value: 4.72e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 694 SFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrqnCNLFSLFFLVMGLISFVTYFFQGF 773
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA----LLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 774 TFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGW 853
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 854 QLTLLLVVIIPLIVLGGIIEMKLLSGQALK-DKKQLEISGKIaTEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKK 932
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRvQEALAELNGRL-QESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 933 AHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEK 1012
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1013 TPEIDSySTEGLKPTLLEGNVKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV 1092
Cdd:COG1132 321 PPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1093 FLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGT 1172
Cdd:COG1132 398 LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEH 1252
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570
....*....|....*....
gi 126927 1253 GTHQQLLAQKGIYFSMVQA 1271
Cdd:COG1132 556 GTHEELLARGGLYARLYRL 574
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1033-1272 |
1.43e-152 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 458.16 E-value: 1.43e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFDCSIAENIAYGDNSRAVshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAG 1272
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
392-628 |
2.97e-152 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 457.00 E-value: 2.97e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 552 LLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 628
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
50-364 |
1.77e-149 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 452.89 E-value: 1.77e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAEASILPSitNQSGPNSTLIISNSsLEEEMAIYAYYYTGIGAGVLIVAY 129
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITG--NSSGLNSSAGPFEK-LEEEMTLYAYYYLIIGAIVLITAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:cd18558 78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:cd18558 158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:cd18558 238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
120-629 |
3.32e-147 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 462.00 E-value: 3.32e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 120 IGAGVLIVAYIQVSL-----WCLA-AGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGI-GDKIGM 191
Cdd:COG2274 198 LAIGLLLALLFEGLLrllrsYLLLrLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLtGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 192 FFQSITTFLAGFIIGFISgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQK 271
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYS-PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESR 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 272 ELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF--SIGHLAP 349
Cdd:COG2274 356 FRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 350 NIEAFANARGAAFEIFKIIDNEPSIDSFSTKGyKPDSIMGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSG 429
Cdd:COG2274 434 LLQRFQDAKIALERLDDILDLPPEREEGRSKL-SLPRLKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 430 CGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAY 509
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 510 DFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLS 589
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 126927 590 TVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQT 629
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
138-625 |
5.60e-141 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 445.71 E-value: 5.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVI 217
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 218 LAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASIS 297
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 298 IGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLtvffSILLGTFSIGHLAPNIEAFAN----ARGAAFEIFKIIDNEPS 373
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPN 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 374 IDSfsTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSID 453
Cdd:TIGR00958 464 IPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 454 GQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGG 533
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAalDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDE 613
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
490
....*....|..
gi 126927 614 LMREKGIYFKLV 625
Cdd:TIGR00958 700 LMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
699-1016 |
6.17e-139 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 425.33 E-value: 6.17e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 699 LNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNcNLFSLFFLVMGLISFVTYFFQGFTFGKA 778
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEA-NFWALMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 779 GEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLL 858
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 859 LVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGI 938
Cdd:cd18578 160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 939 TFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEI 1016
Cdd:cd18578 240 GFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
141-628 |
1.05e-134 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 424.11 E-value: 1.05e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 141 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAV 220
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 221 SPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:TIGR02204 168 VPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLGTfSIGHLAPNIEAFANARGAAFEIFKIIDNEPSIDSFST 379
Cdd:TIGR02204 248 VIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQfVFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAH 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 380 KGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT 459
Cdd:TIGR02204 327 PKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQ 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 460 INVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIA 539
Cdd:TIGR02204 407 LDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG 566
|
....*....
gi 126927 620 IYFKLVMTQ 628
Cdd:TIGR02204 567 LYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
677-1270 |
7.11e-133 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 423.86 E-value: 7.11e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 677 ERRLSMKEAVDEDVPLVSFWRILnlnLSEWPYLLVGVLCAVINGCIQ---PVFA-IVFSRIVGvfsrDDDHETKrqncNL 752
Cdd:COG2274 129 EPTPEFDKRGEKPFGLRWFLRLL---RRYRRLLLQVLLASLLINLLAlatPLFTqVVIDRVLP----NQDLSTL----WV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 753 FSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLaSDASSVKGAMGARLA 832
Cdd:COG2274 198 LAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 833 VVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLsgqALKDKKQLEISGKIAT---EAIENFRTIVSLT 909
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL---RRLSREESEASAKRQSllvETLRGIETIKALG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 910 REQKFETMYAQsLQVPYRNAMKKAHVFGITFS-FTQAMMYFSYAACFRFGAYLVAQQLMTFenVMLV-FSAVVFGAMAA- 986
Cdd:COG2274 352 AESRFRRRWEN-LLAKYLNARFKLRRLSNLLStLSGLLQQLATVALLWLGAYLVIDGQLTL--GQLIaFNILSGRFLAPv 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 987 GNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLlEGNVKFNGVQFNYPTRpNIPVLQGLSLEVKKGQTLAL 1066
Cdd:COG2274 429 AQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRL-KGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAI 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1067 VGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRA 1146
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEA 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1147 AKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCI 1226
Cdd:COG2274 585 ARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVI 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 126927 1227 VIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:COG2274 665 IIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
50-364 |
1.15e-128 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 397.62 E-value: 1.15e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKaeasilpsitnqsgpNSTLIISNSSLEEEMAIYAYYYTGIGAGVLIVAY 129
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTD---------------FGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:cd18577 66 IQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:cd18577 146 SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:cd18577 226 KGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
681-1269 |
5.16e-127 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 408.34 E-value: 5.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 681 SMKEAVDEDV---PLVsfWRILNLNLSEWPYLLVGVL---CAVINGCIQPVF-AIVFSRIVGVFSRDDdhetkrqncnlF 753
Cdd:TIGR00958 134 SEKEAEQGQSetaDLL--FRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYtGRVIDTLGGDKGPPA-----------L 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 754 SLFFLVMGLISFVTYFFQGF---TFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGAR 830
Cdd:TIGR00958 201 ASAIFFMCLLSIASSVSAGLrggSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 831 LAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLsgQALKDKKQLEI--SGKIATEAIENFRTIVSL 908
Cdd:TIGR00958 279 VNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRY--QLLSEELQEAVakANQVAEEALSGMRTVRSF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 909 TRE----QKFETMYAQSLQVPYRNAMKKAhVFGITFSFTQAMMYFSYAACfrfGAYLVAQQLMTFEN-VMLVFSAVVFGA 983
Cdd:TIGR00958 357 AAEegeaSRFKEALEETLQLNKRKALAYA-GYLWTTSVLGMLIQVLVLYY---GGQLVLTGKVSSGNlVSFLLYQEQLGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 984 mAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSysTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQT 1063
Cdd:TIGR00958 433 -AVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEV 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1064 LALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEI 1143
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEI 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1144 VRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEalDKAREGR 1223
Cdd:TIGR00958 588 MAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASR 665
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 126927 1224 TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMV 1269
Cdd:TIGR00958 666 TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
709-1006 |
8.64e-122 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 379.70 E-value: 8.64e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVGVF----------------SRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQG 772
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssglnSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 773 FTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYG 852
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 853 WQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKK 932
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 933 AHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLM-TFENVMLVFSAVVFGAMAAGNTSSFAPdYAKAKVSASHI 1006
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYsIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
737-1265 |
8.04e-116 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 373.65 E-value: 8.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 737 FSRDDDHETKRqncnLFSLFFLVMGLISFVTyFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRL 816
Cdd:TIGR02204 49 FSKDSSGLLNR----YFAFLLVVALVLALGT-AARFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 817 ASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIAT 896
Cdd:TIGR02204 122 TTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 897 EAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF-ENVMLV 975
Cdd:TIGR02204 202 ETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAgTLGQFV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 976 FSAVvFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLS 1055
Cdd:TIGR02204 282 FYAV-MVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1056 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdNS 1135
Cdd:TIGR02204 361 LTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG-RP 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1136 RAvSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEA 1215
Cdd:TIGR02204 440 DA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 126927 1216 LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR02204 519 LETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLY 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
126-630 |
4.59e-115 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 371.36 E-value: 4.59e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 126 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFII 205
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 206 GFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKN 285
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 286 VGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLApNIEA-FANARGAAFEI 364
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLT-NVNApMQRGLAAAESL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 365 FKIIDNEPSIDsfsTKGYKPDSIMGNLEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD 444
Cdd:TIGR02203 308 FTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 445 PLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGR-EDVTMDEIEKAVKEANAYDFIMKLPHQFDTLV 523
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 524 GERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 603
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
490 500
....*....|....*....|....*..
gi 126927 604 VIVEQGNHDELMREKGIYFKLVMTQTR 630
Cdd:TIGR02203 544 RIVERGTHNELLARNGLYAQLHNMQFR 570
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
262-636 |
1.65e-112 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 365.68 E-value: 1.65e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 262 TVIAFGGQQKELERYNKNLEEAKNVGIKKAITAS---------ISIGIAYLLVYASYAlafwygtslVLSNEYSIGEVlt 332
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGDF-- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 333 vffsILLGTFSIGHLAP-NIEAFANA--RGAAFEI---FKIIDNEPSIDSfstkgyKPDSIM-----GNLEFKNVHFNY- 400
Cdd:COG5265 299 ----VLVNAYLIQLYIPlNFLGFVYReiRQALADMermFDLLDQPPEVAD------APDAPPlvvggGEVRFENVSFGYd 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 401 PSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFA 480
Cdd:COG5265 369 PER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFN 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:COG5265 446 DTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 561 DTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIEP 636
Cdd:COG5265 526 DSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEE 601
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
132-628 |
3.93e-109 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 355.87 E-value: 3.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 132 VSLWCLA--AGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDD------------VSKINDG---IGDKIGMFFQ 194
Cdd:PRK11176 84 ISSYCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREGasiIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 195 SittflagfiigfisgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELE 274
Cdd:PRK11176 164 S---------------WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 275 RYNKNLEEAKNVGIKKAITASISIGIAYLLvyASYALAFwygtSLVLSNEYSIGEVL-----TVFFSILlgtfsIGHLAP 349
Cdd:PRK11176 229 RFDKVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAF----VLYAASFPSVMDTLtagtiTVVFSSM-----IALMRP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 350 -----NIEA-FANARGAAFEIFKIIDNEPSIDsfsTKGYKPDSIMGNLEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVA 423
Cdd:PRK11176 298 lksltNVNAqFQRGMAACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 424 LVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDV-TMDEIEKA 502
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 503 VKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTI 582
Cdd:PRK11176 454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 126927 583 VIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 628
Cdd:PRK11176 534 VIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
694-1265 |
8.04e-109 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 354.41 E-value: 8.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 694 SFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIV-GVFSRDDDHETKRQNCNLFSLFfLVMGLISFVTYFFQG 772
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVIGLA-VLRGICSFVSTYLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 773 FTFGKAgeILTKRVRymVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYG 852
Cdd:TIGR02203 80 WVSNKV--VRDIRVR--MFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 853 WQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKK 932
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 933 AHVFGITFSFTQ-----AMMYFSYAACFRFGA-YLVAQQLMTFENVML-VFSAVvfgamaaGNTSSFAPDYAKAKVSASH 1005
Cdd:TIGR02203 234 TSAGSISSPITQliaslALAVVLFIALFQAQAgSLTAGDFTAFITAMIaLIRPL-------KSLTNVNAPMQRGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1006 IIRIIEKTPEIDsysTEGLKPTLLEGNVKFNGVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY 1085
Cdd:TIGR02203 307 LFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1086 DPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnSRAVSHEEIVRAAKEANIHQFIDSLPDKYNT 1165
Cdd:TIGR02203 383 EPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1166 RVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIE 1245
Cdd:TIGR02203 462 PIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMD 541
|
570 580
....*....|....*....|
gi 126927 1246 NGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR02203 542 DGRIVERGTHNELLARNGLY 561
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
391-624 |
1.09e-108 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 341.52 E-value: 1.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1033-1265 |
2.01e-108 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 340.75 E-value: 2.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
391-624 |
6.02e-104 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 328.42 E-value: 6.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNY-PSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREII 469
Cdd:cd03253 1 IEFENVTFAYdPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPK 549
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 550 ILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1008-1268 |
9.66e-104 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 341.80 E-value: 9.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1008 RIIEKTPEI-DSYSTEGLKPTllEGNVKFNGVQFNYptRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD 1086
Cdd:COG5265 334 DLLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1087 PMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdnsRA-VSHEEIVRAAKEANIHQFIDSLPDKYNT 1165
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG---RPdASEEEVEAAARAAQIHDFIESLPDGYDT 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1166 RVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIE 1245
Cdd:COG5265 487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLE 566
|
250 260
....*....|....*....|...
gi 126927 1246 NGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:COG5265 567 AGRIVERGTHAELLAQGGLYAQM 589
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
138-619 |
5.33e-102 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 335.57 E-value: 5.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVI 217
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 218 LAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKnvgikkAIT---- 293
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFR------KRTmkvl 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 294 --ASISIGIAYLLVYASYALAFWY-GTSLvlsneysIGEVLTVF--FSILLgtfsighLAPniEAF-------------A 355
Cdd:COG4988 239 rvAFLSSAVLEFFASLSIALVAVYiGFRL-------LGGSLTLFaaLFVLL-------LAP--EFFlplrdlgsfyharA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 356 NARGAAFEIFKIIDNEPSIDSFSTKGYKPDSImGNLEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTT 435
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 436 VQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKL 515
Cdd:COG4988 380 LNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAAL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 516 PHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNAD 595
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
|
490 500
....*....|....*....|....
gi 126927 596 VIAGFDGGVIVEQGNHDELMREKG 619
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1033-1271 |
3.63e-100 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 318.41 E-value: 3.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQA 1271
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
389-619 |
8.40e-100 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 316.86 E-value: 8.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 GNLEFKNVHFNYpsRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 549 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
316-628 |
1.09e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 327.30 E-value: 1.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 316 GTSLVLSNEYSIGEVLT-VFFSILLgtfsIGHLaPNIEAFAN----ARGAAFEIFKIIDNEPSIDSfstkgyKPDSI--- 387
Cdd:PRK13657 261 GAALVQKGQLRVGEVVAfVGFATLL----IGRL-DQVVAFINqvfmAAPKLEEFFEVEDAVPDVRD------PPGAIdlg 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 --MGNLEFKNVHFNYPSRSevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYL 465
Cdd:PRK13657 330 rvKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALV 545
Cdd:PRK13657 408 RRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 546 RNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLV 625
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
...
gi 126927 626 MTQ 628
Cdd:PRK13657 568 RAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1031-1263 |
1.44e-98 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 313.78 E-value: 1.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1031 GNVKFNGVQFNYptRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH 1110
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1111 LGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1191 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
757-1265 |
5.74e-96 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 319.66 E-value: 5.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 757 FLVMGLI------SFVTYFFQGFTFGKageiLTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGAR 830
Cdd:PRK11176 69 LVVIGLMilrgitSFISSYCISWVSGK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 831 LAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVlggiIEMKLLSG---------------------QALKDKKQLE 889
Cdd:PRK11176 143 LITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVS----IAIRVVSKrfrnisknmqntmgqvttsaeQMLKGHKEVL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 890 ISGKIATEaIENFRTIVSLTREQKFETMYAQSLQVPyrnamkkahVFGITFSFtqAMMYFSYAAcfrfgaylvaqqlmTF 969
Cdd:PRK11176 219 IFGGQEVE-TKRFDKVSNRMRQQGMKMVSASSISDP---------IIQLIASL--ALAFVLYAA--------------SF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 970 ENVMLVFSA----VVFGAMAA--------GNTSSfapDYAKAKVSASHIIRIIEKTPEIDsystEG-LKPTLLEGNVKFN 1036
Cdd:PRK11176 273 PSVMDTLTAgtitVVFSSMIAlmrplkslTNVNA---QFQRGMAACQTLFAILDLEQEKD----EGkRVIERAKGDIEFR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1037 GVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQ 1116
Cdd:PRK11176 346 NVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1117 EPILFDCSIAENIAYGDNSRaVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:PRK11176 425 NVHLFNDTIANNIAYARTEQ-YSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1197 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
697-1263 |
1.47e-92 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 309.77 E-value: 1.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 697 RILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIV-GVFsrdDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTF 775
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLI---IGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 776 gKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLasdassVKG--AMG---AR------LAVVTqnvanlgTG 844
Cdd:COG4988 84 -RAAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLL------TEGveALDgyfARylpqlfLAALV-------PL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 845 VILSLVYG--WQLTLLLVVIIPLIVLGGIiemklLSGQALKDK--KQLEISGKIATEAIENFR---TIVSLTREQKF-ET 916
Cdd:COG4988 148 LILVAVFPldWLSGLILLVTAPLIPLFMI-----LVGKGAAKAsrRQWRALARLSGHFLDRLRgltTLKLFGRAKAEaER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 917 MYAQSLQvpYRNA-MKkahVFGITF--SFT-QAMMYFSYAAC-FRFGAYLVAQQlMTFENVMLV-FSAVVFgamaagnts 990
Cdd:COG4988 223 IAEASED--FRKRtMK---VLRVAFlsSAVlEFFASLSIALVaVYIGFRLLGGS-LTLFAALFVlLLAPEF--------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 991 sFAP------DY---AKAKVSASHIIRIIEKTPEIDSYSTEGLkPTLLEGNVKFNGVQFNYPTRPniPVLQGLSLEVKKG 1061
Cdd:COG4988 288 -FLPlrdlgsFYharANGIAAAEKIFALLDAPEPAAPAGTAPL-PAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1062 QTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRAVSHE 1141
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1142 EIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE 1221
Cdd:COG4988 442 ELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 126927 1222 GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
138-624 |
2.54e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 306.31 E-value: 2.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVskindgigDKIGMFF---------QSITTFLAGFIIGFI 208
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlrvllpllvALLVILAAVAFLAFF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 209 SgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKEL-QAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYN---KNLEEAK 284
Cdd:COG4987 154 S-PALALVLALGLLLAGLLLPLLAARLGRRAGRRLaAARAALRARLTDLLQGAAELAAYGALDRALARLDaaeARLAAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 285 NvgiKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSiGEVLTVFFSILLGTFSIghLAPNIEAFAN---ARGAA 361
Cdd:COG4987 233 R---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAQHlgrVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 362 FEIFKIIDNEPSIDSFSTKGYKPDSimGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQR 441
Cdd:COG4987 307 RRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 442 LYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDT 521
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 522 LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFD 601
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|...
gi 126927 602 GGVIVEQGNHDELMREKGIYFKL 624
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1024-1249 |
7.19e-89 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 287.06 E-value: 7.19e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1024 LKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN 1103
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1104 VQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIA 1183
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1249
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
149-629 |
3.41e-87 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 298.58 E-value: 3.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 149 KFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGIGDK-----IGMFFqsITTFLAgfIIGFISGwKLTLVILAVSPL 223
Cdd:TIGR01846 217 RLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSaltvvLDLLF--VVVFLA--VMFFYSP-TLTGVVIGSLVC 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 224 IGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYL 303
Cdd:TIGR01846 291 YALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 304 LVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTFS--IGHLAPNIEAFANArGAAFEIFKIIDNEPSIDSFSTKG 381
Cdd:TIGR01846 371 IQKLTFAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQQT-GIALERLGDILNSPTEPRSAGLA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 382 YKPDsIMGNLEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN 461
Cdd:TIGR01846 448 ALPE-LRGAITFENIRFRYAPDSPE-VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 VRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIA 541
Cdd:TIGR01846 526 PAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 542 RALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIY 621
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
....*...
gi 126927 622 FKLVMTQT 629
Cdd:TIGR01846 686 ARLWQQQS 693
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
785-1270 |
1.31e-86 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 293.21 E-value: 1.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 785 RVRymVFKSMLRQDISWFddHKNSTGSLTTRLASDASSVKGAMgarLAVVTQNVANLGTGVILSLVYGW-QLTLLLVVII 863
Cdd:COG4987 91 RVR--LYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFfSPALALVLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 864 PLIVLGGIIemKLLSGQALK--DKKQLEISGKIATEAIENFRTIVSLT---REQKFETMYAQSLQVPYRNAMKKAHVFGI 938
Cdd:COG4987 164 GLLLAGLLL--PLLAARLGRraGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDAAEARLAAAQRRLARLSAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 939 TFSFTQAMMYFSYAACFRFGAYLVAQQlmTFENVMLVfsAVVFGAMAA----GNTSSFAPDYAKAKVSASHIIRIIEKTP 1014
Cdd:COG4987 242 AQALLQLAAGLAVVAVLWLAAPLVAAG--ALSGPLLA--LLVLAALALfealAPLPAAAQHLGRVRAAARRLNELLDAPP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1015 EIDSYSTEGLKPTllEGNVKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFL 1094
Cdd:COG4987 318 AVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1095 DGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNsrAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQL 1174
Cdd:COG4987 395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1175 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
490
....*....|....*.
gi 126927 1255 HQQLLAQKGIYFSMVQ 1270
Cdd:COG4987 553 HEELLAQNGRYRQLYQ 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
391-628 |
2.20e-85 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 277.83 E-value: 2.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 628
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
46-374 |
6.98e-84 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 276.64 E-value: 6.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 46 DKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTkaeasilpsitnqsgpnstlIISNSSLEEEMAIYAYYYTGIGAGVL 125
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFS--------------------LPDDDELRSEANFWALMFLVLAIVAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 126 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFD--VHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGF 203
Cdd:cd18578 67 IAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 204 IIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEA 283
Cdd:cd18578 147 IIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 284 KNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIG---HLAPNIeafANARGA 360
Cdd:cd18578 227 LKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGqafSFAPDI---AKAKAA 303
|
330
....*....|....
gi 126927 361 AFEIFKIIDNEPSI 374
Cdd:cd18578 304 AARIFRLLDRKPEI 317
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
384-605 |
1.84e-83 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 272.04 E-value: 1.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 384 PDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR 463
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 YLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARA 543
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVI 605
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
50-342 |
1.28e-82 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 271.44 E-value: 1.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKaeasilpsitnqsgpnstliiSNSSLEEEMAIYAYYYTGIGAGVLIVAY 129
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLP---------------------DGDPETQALNVYSLALLLLGLAQFILSF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:pfam00664 60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:pfam00664 140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGE--VLTVFFSILLGTF 342
Cdd:pfam00664 220 KAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
847-1272 |
1.17e-81 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 279.92 E-value: 1.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 847 LSLVYGWQLTLLLVVI-IPLIVLGGIIEMKLLSGQALKDKKQLEISGKiATEAIENFRTIVSLTR-EQKFETM--YAQSL 922
Cdd:PRK13657 150 LALFMNWRLSLVLVVLgIVYTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRiEAETQALrdIADNL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 923 ---QVPYRNAMkkAHVFGIT-FSFTQAMMyfsyaACFRFGAYLVAQQLMTfenVMLVFSAVVFGAMAAG---NTSSFAPD 995
Cdd:PRK13657 229 laaQMPVLSWW--ALASVLNrAASTITML-----AILVLGAALVQKGQLR---VGEVVAFVGFATLLIGrldQVVAFINQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 996 YAKAKVSASHIIRIIEKTPEIDSysTEGLK-PTLLEGNVKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:PRK13657 299 VFMAAPKLEEFFEVEDAVPDVRD--PPGAIdLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1075 STVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQ 1154
Cdd:PRK13657 375 STLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHD 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1155 FIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1234
Cdd:PRK13657 453 FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLST 532
|
410 420 430
....*....|....*....|....*....|....*...
gi 126927 1235 IQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAG 1272
Cdd:PRK13657 533 VRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
694-1265 |
1.33e-81 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 283.37 E-value: 1.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 694 SFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSrivgvfsrddDHETKRQNCNLFSLFFLVMGLisfvTYFFQGF 773
Cdd:TIGR03796 144 ALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFV----------DEILVQGRQDWLRPLLLGMGL----TALLQGV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 774 TFGKAGEILTKRVRYM-------VFKSMLRQDISWFDdhKNSTGSLTTRLASdASSVKGAMGARLAVVTQNVANLGTGVI 846
Cdd:TIGR03796 210 LTWLQLYYLRRLEIKLavgmsarFLWHILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYAL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 847 LSLVYGWQLTLLLVVI--IPLIVLGGIIEMKLLSGQALkdkkQLEiSGKIATEAIENFRTIVSLTRE-------QKFETM 917
Cdd:TIGR03796 287 LMLLYDPVLTLIGIAFaaINVLALQLVSRRRVDANRRL----QQD-AGKLTGVAISGLQSIETLKASglesdffSRWAGY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 918 YAQSLqvpyrNAMKKAHVFGITFS-FTQAMMYFSYAACFRFGAYLVAQQLMT------FENVMLVFSAVVFGAMAAGNT- 989
Cdd:TIGR03796 362 QAKLL-----NAQQELGVLTQILGvLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTl 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 990 SSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEglKPTLLEGNVKFNGVQFNYpTRPNIPVLQGLSLEVKKGQTLALVGS 1069
Cdd:TIGR03796 437 QELEGDLNRLDDVLRNPVDPLLEEPEGSAATSE--PPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1070 SGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKE 1149
Cdd:TIGR03796 514 SGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKD 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1150 ANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdkAREGRTCIVIA 1229
Cdd:TIGR03796 592 AAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVA 669
|
570 580 590
....*....|....*....|....*....|....*.
gi 126927 1230 HRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR03796 670 HRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
391-603 |
3.91e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 260.39 E-value: 3.91e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 126927 551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 603
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1033-1270 |
4.87e-80 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 262.81 E-value: 4.87e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHL 1111
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVSQEPILFDCSIAENIAYGDNsrAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1192 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1033-1248 |
2.39e-79 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 258.08 E-value: 2.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFDCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 1192
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGK 1248
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
194-627 |
8.75e-78 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 268.68 E-value: 8.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFLAGFII---GFISGWKLTLVilavspLIGLSSALW--AKVLTSFTnKELQA-----YAKAGAVAEEVLAAIRTV 263
Cdd:TIGR01192 136 QHLATFVALFLLiptAFAMDWRLSIV------LMVLGILYIliAKLVMQRT-KNGQAavehhYHNVFKHVSDSISNVSVV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 264 IAFG---GQQKELERYNKNLEEAKNVGIKKAITASisiGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILL 339
Cdd:TIGR01192 209 HSYNrieAETSALKQFTNNLLSAQYPVLDWWALAS---GLNRMASTISMMCILVIGTVLVIKGELSVGEVIAfIGFANLL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 340 gtfsIGHLaPNIEAFAN----ARGAAFEIFKIID-----NEPSiDSFSTKGYKpdsimGNLEFKNVHFNYPSRSevQILK 410
Cdd:TIGR01192 286 ----IGRL-DQMSGFITqifeARAKLEDFFDLEDsvfqrEEPA-DAPELPNVK-----GAVEFRHITFEFANSS--QGVF 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 411 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG 490
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLG 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 491 REDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQA 570
Cdd:TIGR01192 433 REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKN 512
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 571 ALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMT 627
Cdd:TIGR01192 513 AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
709-1006 |
2.21e-76 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 255.09 E-value: 2.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSR----DDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTK 784
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 785 RVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIP 864
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 865 LIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQ 944
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 945 AMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHI 1006
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
794-1270 |
4.24e-76 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 266.82 E-value: 4.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 794 MLRQDISWFDDHknSTGSLTTRlasdASSVKgAMGARLAVVTQNVANLGTGVILSLV----YGWQLTLLLVVIIPLIVLG 869
Cdd:TIGR03797 219 LLRLPVSFFRQY--STGDLASR----AMGIS-QIRRILSGSTLTTLLSGIFALLNLGlmfyYSWKLALVAVALALVAIAV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 870 -GIIEMKLLSgqalKDKKQLEISGKIATEAIENFRTIVSLtR----EQKFETMYAQ--SLQVpyRNAMKKAHVFGITFSF 942
Cdd:TIGR03797 292 tLVLGLLQVR----KERRLLELSGKISGLTVQLINGISKL-RvagaENRAFARWAKlfSRQR--KLELSAQRIENLLTVF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 943 TQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAvvFGAMAAGNTS---------SFAPDYAKAKvsashiiRIIEKT 1013
Cdd:TIGR03797 365 NAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTA--FGSFSGAVTQlsntlisilAVIPLWERAK-------PILEAL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1014 PEIDSYSTEglkPTLLEGNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV 1092
Cdd:TIGR03797 436 PEVDEAKTD---PGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1093 FLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAyGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGT 1172
Cdd:TIGR03797 511 FYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVIENGKVKEH 1252
Cdd:TIGR03797 588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQ 665
|
490
....*....|....*...
gi 126927 1253 GTHQQLLAQKGIYFSMVQ 1270
Cdd:TIGR03797 666 GTYDELMAREGLFAQLAR 683
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
1029-1270 |
6.35e-74 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 260.83 E-value: 6.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1029 LEGNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL 1107
Cdd:TIGR01846 452 LRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1108 RAHLGIVSQEPILFDCSIAENIAYGDNsrAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARA 1187
Cdd:TIGR01846 530 RRQMGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1188 LVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS 1267
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
...
gi 126927 1268 MVQ 1270
Cdd:TIGR01846 688 LWQ 690
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
709-1246 |
3.03e-71 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 262.66 E-value: 3.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDhetkrQNCNLFSLffLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:PTZ00265 62 LGVSFVCATISGGTLPFFVSVFGVIMKNMNLGEN-----VNDIIFSL--VLIGIFQFILSFISSFCMDVVTTKILKTLKL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 789 MVFKSMLRQDISWfddHKNSTGS-LTTRLASDASSVKGAMGAR-LAVVTQNVANLGTgVILSLVYGWQLTLLLVVIIPLI 866
Cdd:PTZ00265 135 EFLKSVFYQDGQF---HDNNPGSkLTSDLDFYLEQVNAGIGTKfITIFTYASAFLGL-YIWSLFKNARLTLCITCVFPLI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 867 VLGGIIEMKLLSgqaLKDKKQLEISGK---IATEAIENFRTIVSLTRE----QKF---ETMYAQSLQVPyrNAMKKAHVf 936
Cdd:PTZ00265 211 YICGVICNKKVK---INKKTSLLYNNNtmsIIEEALVGIRTVVSYCGEktilKKFnlsEKLYSKYILKA--NFMESLHI- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 937 GITFSFTQAmmyfSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFA--------PDYAKAKVSASHIIR 1008
Cdd:PTZ00265 285 GMINGFILA----SYAFGFWYGTRIIISDLSNQQPNNDFHGGSVISILLGVLISMFMltiilpniTEYMKSLEATNSLYE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1009 IIEKTPEIDSySTEGLKPTLLEgNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM 1088
Cdd:PTZ00265 361 IINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1089 AGSVFL-DGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAY------------------------GDNSR------- 1136
Cdd:PTZ00265 439 EGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakc 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1137 ------------------------AVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:PTZ00265 519 agdlndmsnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNP 598
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1193 HILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQNADLIVVIEN 1246
Cdd:PTZ00265 599 KILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
709-984 |
3.64e-70 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 236.39 E-value: 3.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET--QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 789 MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:pfam00664 79 KLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 869 GGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMY 948
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 126927 949 FSYAACFRFGAYLVAQQLMTFEN--VMLVFSAVVFGAM 984
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
389-609 |
2.06e-69 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 232.09 E-value: 2.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 GNLEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 549 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1031-1249 |
2.78e-69 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 231.71 E-value: 2.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1031 GNVKFNGVQFNYPTRPnIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH 1110
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1111 LGIVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1191 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1249
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
371-1270 |
9.37e-69 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 254.87 E-value: 9.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 371 EPsiDSFSTKGYKPDSimGN-LEFKNVHFNYpSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGV 449
Cdd:TIGR00957 620 EP--DSIERRTIKPGE--GNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 450 VSIDGqdirtiNVRYlreiigvVSQEPVLFATTIAENIRYGREdvTMDEIEKAVKEANAY--DFIMkLPHQFDTLVGERG 527
Cdd:TIGR00957 695 VHMKG------SVAY-------VPQQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKG 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 528 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTEseaVVQAALDKA------REGRTTIVIAHRLSTVRNADVIAGFD 601
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMS 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 602 GGVIVEQGNHDELMREKGIYFKLVMTQTRGNE---IEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYR----SVHRKQ 674
Cdd:TIGR00957 836 GGKISEMGSYQELLQRDGAFAEFLRTYAPDEQqghLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRqlsaSSSDSG 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 675 DQERRLSMKEAVDEDVPLVSFWRILNLNLSE---------WPYLLVGVLCAVINGCI----QPVFAIVFSRIVGVFSRDD 741
Cdd:TIGR00957 916 DQSRHHGSSAELQKAEAKEETWKLMEADKAQtgqvelsvyWDYMKAIGLFITFLSIFlfvcNHVSALASNYWLSLWTDDP 995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 742 DHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDAS 821
Cdd:TIGR00957 996 MVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELD 1073
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 822 SVKGAMGARLAVVTQNVANLGTGVILSLVygwQLTLLLVVIIPLIVLGGIIE-MKLLSGQALKDKKQLEISGKIA--TEA 898
Cdd:TIGR00957 1074 TVDSMIPPVIKMFMGSLFNVIGALIVILL---ATPIAAVIIPPLGLLYFFVQrFYVASSRQLKRLESVSRSPVYShfNET 1150
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 899 IENFRTIVSLTREQKFEtmYAQSLQVpyrNAMKKAhvfgitfsftqammYFSYAACFRFgaylVAQQLMTFENVMLVFSA 978
Cdd:TIGR00957 1151 LLGVSVIRAFEEQERFI--HQSDLKV---DENQKA--------------YYPSIVANRW----LAVRLECVGNCIVLFAA 1207
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 979 VvfgaMAAGNTSSFAPDYAKAKVSAS--------HIIRI-------IEKTPEIDSYS-TEGLKPTLLE-----------G 1031
Cdd:TIGR00957 1208 L----FAVISRHSLSAGLVGLSVSYSlqvtfylnWLVRMssemetnIVAVERLKEYSeTEKEAPWQIQetappsgwpprG 1283
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1032 NVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH 1110
Cdd:TIGR00957 1284 RVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK 1361
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1111 LGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:TIGR00957 1362 ITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1191 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
160-628 |
6.32e-68 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 242.94 E-value: 6.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 160 GWFDVHDVGELNTRlTDDVSKINDGIGDKIgmffqsITTFLAGFI----IG--FISGWKLTLV---ILAVSPLIGLSSAL 230
Cdd:TIGR03797 225 SFFRQYSTGDLASR-AMGISQIRRILSGST------LTTLLSGIFallnLGlmFYYSWKLALVavaLALVAIAVTLVLGL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 231 WAkvltsfTNKELQAYAKAGAVAEEVLAAIRTVIAF---GGQQKELERYNKNLEEAKNVGIKKAITASI-SIGIAYLLVY 306
Cdd:TIGR03797 298 LQ------VRKERRLLELSGKISGLTVQLINGISKLrvaGAENRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 307 ASYALaFWYGTSLVLSNEYSIGEVLTvfFSILLGTFSIGhlapnIEAFANARGAAFEIF-------KIIDNEPSIDSFST 379
Cdd:TIGR03797 372 TSAAL-FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA-----VTQLSNTLISILAVIplwerakPILEALPEVDEAKT 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 380 KgykPDSIMGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT 459
Cdd:TIGR03797 444 D---PGKLSGAIEVDRVTFRYRPDGP-LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAG 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 460 INVRYLREIIGVVSQEPVLFATTIAENIrYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIA 539
Cdd:TIGR03797 520 LDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLL 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRttIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREG 676
|
....*....
gi 126927 620 IYFKLVMTQ 628
Cdd:TIGR03797 677 LFAQLARRQ 685
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
190-597 |
2.43e-66 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 234.10 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 190 GMFFQSITTFLAGFIIGFISgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFG-- 267
Cdd:TIGR02857 124 QLVLAVIVPLAILAAVFPQD-WISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGra 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 268 -GQQKELERYNKNLEEAKNVGIKKAITASI------SIGIAYLLVYasyalafwYGTSLVlsneysiGEVLTVF--FSIL 338
Cdd:TIGR02857 203 kAQAAAIRRSSEEYRERTMRVLRIAFLSSAvlelfaTLSVALVAVY--------IGFRLL-------AGDLDLAtgLFVL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 339 LgtfsighLAPniEAF-------------ANARGAAFEIFKIIDNEPSIdsFSTKGYKPDSIMGNLEFKNVHFNYPSRSE 405
Cdd:TIGR02857 268 L-------LAP--EFYlplrqlgaqyharADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAE 485
Cdd:TIGR02857 337 A--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 486 NIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 565
Cdd:TIGR02857 415 NIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
410 420 430
....*....|....*....|....*....|..
gi 126927 566 AVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:TIGR02857 495 AEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
389-610 |
1.63e-65 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 220.83 E-value: 1.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 GNLEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFATTIAENI----RYgredvTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 610
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1030-1261 |
1.81e-65 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 232.72 E-value: 1.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1030 EGNVKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:COG4618 328 KGRLSVENLTVVPPGSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILFDCSIAENIA-YGDnsraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARAL 1188
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1189 VRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1031-1254 |
5.98e-64 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 216.59 E-value: 5.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1031 GNVKFNGVQFNYptRPNI-PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILFDCSIAENIA----YGDnsravshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 1185
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1186 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
134-621 |
6.86e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 228.44 E-value: 6.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 134 LWCLAAGRQIH-KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS-GW 211
Cdd:PRK10789 58 VLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQiSW 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 212 KLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEA--KNVGIK 289
Cdd:PRK10789 138 QLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkKNMRVA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 290 KA-----ITASISIGIAYLLvyasyalAFWYGTSLVLSNEYSIGEvLTVFFsILLGTFSIGHLAP----NIEAfanaRGA 360
Cdd:PRK10789 218 RIdarfdPTIYIAIGMANLL-------AIGGGSWMVVNGSLTLGQ-LTSFV-MYLGLMIWPMLALawmfNIVE----RGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 361 AF--EIFKIIDNEPSIDSfstkGYKP-DSIMGNLEFKNVHFNYPsRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ 437
Cdd:PRK10789 285 AAysRIRAMLAEAPVVKD----GSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 438 LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPH 517
Cdd:PRK10789 360 LIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQ 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 518 QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEI 519
|
490 500
....*....|....*....|....
gi 126927 598 AGFDGGVIVEQGNHDELMREKGIY 621
Cdd:PRK10789 520 LVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
391-1271 |
6.68e-63 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 236.03 E-value: 6.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEgVVSIDgqdirtinvryLREIIG 470
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIRYGrEDVTMDEIEKAVKeanaydfIMKLPHQFD-------TLVGERGAQLSGGQKQRIAIARA 543
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFG-SDFESERYWRAID-------VTALQHDLDllpgrdlTEIGERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 544 LVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYF 622
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLF 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 623 KLVMtqtrgneiEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQERRLSMKEAVDEDVPLVSfWRIL--- 699
Cdd:PLN03232 834 KKLM--------ENAGKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERETGIIS-WNVLmry 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 700 NLNLSEWPYLLVGVLCAVINgciqPVFAIVFSRIVGVFSRDDDHETKRQncnlfSLFFLVMGLISF----VTyFFQGFTF 775
Cdd:PLN03232 905 NKAVGGLWVVMILLVCYLTT----EVLRVSSSTWLSIWTDQSTPKSYSP-----GFYIVVYALLGFgqvaVT-FTNSFWL 974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 776 GKAGEILTKRVRYMVFKSMLRQDISWFddHKNSTGSLTTRLASDASSVKgamgarlavvtQNVANLGTGVILSLvygWQL 855
Cdd:PLN03232 975 ISSSLHAAKRLHDAMLNSILRAPMLFF--HTNPTGRVINRFSKDIGDID-----------RNVANLMNMFMNQL---WQL 1038
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 856 --TLLLVVIIPLIVLGGIIEMKLLSGQAL-------KDKKQLEISGKIAT-----EAIENFRTIVSLTREQKFETMYAQS 921
Cdd:PLN03232 1039 lsTFALIGTVSTISLWAIMPLLILFYAAYlyyqstsREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKINGKS 1118
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 922 LQVPYRNAMKKAHVFG---ITFSFTQAMMYFSYA--ACFRFG--------AYLVAQQLMTFENVMLVFSAVVFGAMAAGN 988
Cdd:PLN03232 1119 MDNNIRFTLANTSSNRwltIRLETLGGVMIWLTAtfAVLRNGnaenqagfASTMGLLLSYTLNITTLLSGVLRQASKAEN 1198
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 989 TSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLkptllegnVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALV 1067
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGS--------IKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVV 1268
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1068 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI-AYGDNSRAvsheEIVRA 1146
Cdd:PLN03232 1269 GRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDA----DLWEA 1344
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1147 AKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCI 1226
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 126927 1227 VIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG-IYFSMVQA 1271
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHS 1470
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
215-617 |
7.54e-63 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 225.01 E-value: 7.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 215 LVILAVSPLIGLSSALWAKVLTS-------FTNKEL----QAYAKAGAVAEEVLAAIRTVIAFG----GQQKELERYNKN 279
Cdd:COG4618 148 AVLFLFHPLLGLLALVGALVLVAlallnerLTRKPLkeanEAAIRANAFAEAALRNAEVIEAMGmlpaLRRRWQRANARA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 280 LEEAKNVGIKKAITASISIGIAYLLVYASYALAFWygtsLVLSNEYSIGevltVFF--SILLGTFsighLAPnIE----- 352
Cdd:COG4618 228 LALQARASDRAGGFSALSKFLRLLLQSAVLGLGAY----LVIQGEITPG----AMIaaSILMGRA----LAP-IEqaigg 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 353 --AFANARGAAFEIFKIIDNEPSidsfstkgyKPDSIM-----GNLEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALV 425
Cdd:COG4618 295 wkQFVSARQAYRRLNELLAAVPA---------EPERMPlprpkGRLSVENLTVVPPG-SKRPILRGVSFSLEPGEVLGVI 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 426 GNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI-RYGreDVTMDEIEKAVK 504
Cdd:COG4618 365 GPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 505 EANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIV 583
Cdd:COG4618 443 LAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVV 522
|
410 420 430
....*....|....*....|....*....|....
gi 126927 584 IAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG4618 523 ITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
963-1270 |
1.16e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 224.70 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 963 AQQLMTFEN-----VMLVFSA---------------VVFGAMAA--------------GNTSSfapdyakakvSASHIIR 1008
Cdd:PRK11160 247 SQALMILANgltvvLMLWLAAggvggnaqpgalialFVFAALAAfealmpvagafqhlGQVIA----------SARRINE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1009 IIEKTPEIDSYSTEGLKPTllEGNVKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM 1088
Cdd:PRK11160 317 ITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1089 AGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYgdnsravsheeivrAAKEANIHQFIDSL--------- 1159
Cdd:PRK11160 394 QGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEALIEVLqqvglekll 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1160 --PDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN 1237
Cdd:PRK11160 460 edDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
|
330 340 350
....*....|....*....|....*....|...
gi 126927 1238 ADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:PRK11160 540 FDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
126-625 |
2.17e-62 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 227.31 E-value: 2.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 126 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGIGDKIGMFFQSITTFLA-GFI 204
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 205 IGFISGwKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQK-------ELERY- 276
Cdd:TIGR01193 290 LVRQNM-LLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidsEFGDYl 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 277 NKNLEEAKNVGIKKAITASISIGIAYLLVyasyalafWYGTSLVLSNEYSIGEVLTvfFSILLGTF-----SIGHLAPNI 351
Cdd:TIGR01193 369 NKSFKYQKADQGQQAIKAVTKLILNVVIL--------WTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQPKL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 352 EAFANARGAAFEIFkIIDNEpsidsFSTKGYKPDSIM--GNLEFKNVHFNYPSRSEvqILKGLNLKVKSGQTVALVGNSG 429
Cdd:TIGR01193 439 QAARVANNRLNEVY-LVDSE-----FINKKKRTELNNlnGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSG 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 430 CGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG-REDVTMDEIEKAVKEANA 508
Cdd:TIGR01193 511 SGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 509 YDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVIAHRL 588
Cdd:TIGR01193 591 KDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRL 669
|
490 500 510
....*....|....*....|....*....|....*..
gi 126927 589 STVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLV 625
Cdd:TIGR01193 670 SVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
995-1244 |
6.86e-62 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 221.39 E-value: 6.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 995 DYAKAKVSASHIIRIIEKTPEIDSYSTEglKPTLLEGNVKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1075 STVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRAAKEANIHQ 1154
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1155 FIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1234
Cdd:TIGR02857 440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
|
250
....*....|
gi 126927 1235 IQNADLIVVI 1244
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
757-1270 |
2.11e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 221.52 E-value: 2.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 757 FLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGARLAVVTQ 836
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 837 NVANLGTGVILSLVYGWQLTLLLVVIIP--LIVLGgiiemkllsgqalkdkkqleISGKIATEAIENFRTIVSLTREQKF 914
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPavLVVMV--------------------IYQRYSTPIVRRVRAYLADINDGFN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 915 ETMYAQSLQVPYRNAMKkahvFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGnTSSFAP 994
Cdd:PRK10790 209 EVINGMSVIQQFRQQAR----FGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILCGLLMLFGFSASG-TIEVGV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 995 DYA-----------------------KAKVSASHIIRIIEKTPEidSYSTEGLkpTLLEGNVKFNGVQFNYptRPNIPVL 1051
Cdd:PRK10790 284 LYAfisylgrlneplielttqqsmlqQAVVAGERVFELMDGPRQ--QYGNDDR--PLQSGRIDIDNVSFAY--RDDNLVL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1052 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAY 1131
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1132 GdnsRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:PRK10790 438 G---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1212 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:PRK10790 515 IQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
759-1268 |
4.09e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 217.27 E-value: 4.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 759 VMGLISFVTY----FFQGFTFGkAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMG-ARLAV 833
Cdd:PRK10789 41 TMVLIAVVVYllryVWRVLLFG-ASYQLAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGeGVLTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 834 VTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL-----GGIIEMKLLSGQA----LKDKKQleisgkiatEAIENFRT 904
Cdd:PRK10789 118 VDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAImikryGDQLHERFKLAQAafssLNDRTQ---------ESLTSIRM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 905 IVSLTREQKFETMYAQSLQVPYRNAMKKAHV---FGITFSFTQAMmyfSYAACFRFGAYLVAQqlmtfenvmlvfsavvf 981
Cdd:PRK10789 189 IKAFGLEDRQSALFAADAEDTGKKNMRVARIdarFDPTIYIAIGM---ANLLAIGGGSWMVVN----------------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 982 GAMAAGNTSSFA--------PDYAKA-------KVSA--SHIIRIIEKTPEIDsystEGLKPTLLE-GNVKFNGVQFNYP 1043
Cdd:PRK10789 249 GSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAaySRIRAMLAEAPVVK----DGSEPVPEGrGELDVNIRQFTYP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDC 1123
Cdd:PRK10789 325 QTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYGdnSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK10789 404 TVANNIALG--RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1204 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
752-1271 |
1.18e-58 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 216.14 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLaSDASSVKGAMGARL 831
Cdd:TIGR01193 197 IISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRR--TGEIVSRF-TDASSIIDALASTI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 832 AVVTQNVANLgtgVILSLVYGWQ---LTLLLVVIIPLIVLGGIIEMKLLSGQalkDKKQLEISGKIATEAIENF---RTI 905
Cdd:TIGR01193 274 LSLFLDMWIL---VIVGLFLVRQnmlLFLLSLLSIPVYAVIIILFKRTFNKL---NHDAMQANAVLNSSIIEDLngiETI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 906 VSLTREQ--------KFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFsyaacfrfGAYLVAQQLMTFENVmLVFS 977
Cdd:TIGR01193 348 KSLTSEAeryskidsEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWT--------GAYLVMRGKLTLGQL-ITFN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 978 AVV-FGAMAAGNTSSFAPDYAKAKVSAshiIRIIE----KTPEIDSYSTEGLkpTLLEGNVKFNGVQFNYPTrpNIPVLQ 1052
Cdd:TIGR01193 419 ALLsYFLTPLENIINLQPKLQAARVAN---NRLNEvylvDSEFINKKKRTEL--NNLNGDIVINDVSYSYGY--GSNILS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYG 1132
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1133 dNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVV 1212
Cdd:TIGR01193 572 -AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKI 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1213 QEALDKAREgRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQA 1271
Cdd:TIGR01193 651 VNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
168-588 |
5.13e-58 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 209.91 E-value: 5.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 168 GELNTRLTDDVskinDGIGDkigMFFQSITTFLAGFIIGFISgwklTLVILAVSP---LIGLSSALWAKVLTSFT----- 239
Cdd:TIGR02868 110 GDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGAAA----VAAIAVLSVpaaLILAAGLLLAGFVAPLVslraa 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 240 -NKELQAYAKAGAVAEEVLAAIR---TVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWY 315
Cdd:TIGR02868 179 rAAEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 316 GTSLVLSNEYSiGEVLTVFFSILLGTFSI-GHLAPNIEAFANARGAAFEIFKIIDNEPSIDSFSTKGYKPDSIMG-NLEF 393
Cdd:TIGR02868 259 GGPAVADGRLA-PVTLAVLVLLPLAAFEAfAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLEL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 394 KNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVS 473
Cdd:TIGR02868 338 RDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 474 QEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:TIGR02868 416 QDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
410 420 430
....*....|....*....|....*....|....*
gi 126927 554 DEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
360-624 |
4.12e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.44 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 360 AAFEIFKIIDNEPSIdSFSTKGyKPDSIMGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM 439
Cdd:PRK11160 310 SARRINEITEQKPEV-TFPTTS-TAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 440 QRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTmDEIEKAVKEANAYDFIMKLPHQF 519
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 520 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 599
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*
gi 126927 600 FDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
394-1271 |
2.04e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 212.29 E-value: 2.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 394 KNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdgqdirtinvryLREIIGVVS 473
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 474 QEPVLFATTIAENIRYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 554 DEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYFKLVMTQtrGN 632
Cdd:PLN03130 765 DDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN-GPLFQKLMEN--AG 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 633 EIEPGNNAYGSQSDTDASELTSEESKSPLIRRSiyrSVHRKQDQERRLSMKEAVDEDVPLVSfWRIL----NLNLSEWpy 708
Cdd:PLN03130 842 KMEEYVEENGEEEDDQTSSKPVANGNANNLKKD---SSSKKKSKEGKSVLIKQEERETGVVS-WKVLerykNALGGAW-- 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 lLVGVL--CAVINgciqPVFAIVFSRIVGVFSrddDHETKRQNCNLFslFFLVMGLISF----VTyFFQGFTFGKAGEIL 782
Cdd:PLN03130 916 -VVMILflCYVLT----EVFRVSSSTWLSEWT---DQGTPKTHGPLF--YNLIYALLSFgqvlVT-LLNSYWLIMSSLYA 984
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 783 TKRVRYMVFKSMLRQDISWFddHKNSTGSLTTRLASDassvkgamgarLAVVTQNVANLgtgVILSLVYGWQL--TLLLV 860
Cdd:PLN03130 985 AKRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVF---VNMFLGQIFQLlsTFVLI 1048
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 861 VIIPLIVLGGIIEMKLLSGQAL-------KDKKQLEisgkiateaienfrtivSLTREqkfeTMYAQ--------SLQVP 925
Cdd:PLN03130 1049 GIVSTISLWAIMPLLVLFYGAYlyyqstaREVKRLD-----------------SITRS----PVYAQfgealnglSTIRA 1107
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 926 YRNAMKKAHVFGITFS----FTQAMMYfsyaacfrfGAYLVAQQLMTFENVMLVFSA--VVFGAMAAGNTSSFAPDYAKA 999
Cdd:PLN03130 1108 YKAYDRMAEINGRSMDnnirFTLVNMS---------SNRWLAIRLETLGGLMIWLTAsfAVMQNGRAENQAAFASTMGLL 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1000 KVSASHIIRIIEKTPEIDSYSTEGLK---------------PTLLEGN-----------VKFNGVQFNYptRPNIP-VLQ 1052
Cdd:PLN03130 1179 LSYALNITSLLTAVLRLASLAENSLNavervgtyidlpseaPLVIENNrpppgwpssgsIKFEDVVLRY--RPELPpVLH 1256
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI-AY 1131
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdPF 1336
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1132 GDNSRAvsheEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:PLN03130 1337 NEHNDA----DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1212 VQEALDKarEGRTC--IVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS-MVQA 1271
Cdd:PLN03130 1413 IQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMVQS 1473
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
129-635 |
4.08e-55 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 203.03 E-value: 4.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 129 YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFI 208
Cdd:PRK10790 83 YAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 209 SGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKeLQAY-AKAGAVAEEVLAAIRTVIAFGGQQkeleRYNKNLEEAKNVG 287
Cdd:PRK10790 163 LDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRR-VRAYlADINDGFNEVINGMSVIQQFRQQA----RFGERMGEASRSH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 288 IKKAITA----------SISIGIAYLLVyasyALAFWYGtslvLSNEYSIG-EVLTVFFSILlgtfsiGHL-APNIE--- 352
Cdd:PRK10790 238 YMARMQTlrldgfllrpLLSLFSALILC----GLLMLFG----FSASGTIEvGVLYAFISYL------GRLnEPLIEltt 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 353 ---AFANARGAAFEIFKIIDNEpsidsfsTKGYKPDSIM---GNLEFKNVHFNYpsRSEVQILKGLNLKVKSGQTVALVG 426
Cdd:PRK10790 304 qqsMLQQAVVAGERVFELMDGP-------RQQYGNDDRPlqsGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 427 NSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGReDVTMDEIEKAVKEA 506
Cdd:PRK10790 375 HTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 507 NAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 586
Cdd:PRK10790 454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 126927 587 RLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIE 635
Cdd:PRK10790 534 RLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELA 582
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
294-621 |
9.23e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.00 E-value: 9.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 294 ASISIgiAYLLVY--ASY--ALAF-WYGTS---------LVLSNEysigevltvFFSIL--LGTFSigHlapnieAFANA 357
Cdd:PRK11174 257 ASISI--ALVAVYfgFSYlgELNFgHYGTGvtlfagffvLILAPE---------FYQPLrdLGTFY--H------AKAQA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 358 RGAAFEIFKIIDNEpsiDSFSTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvq 437
Cdd:PRK11174 318 VGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTS--- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 438 LMQRL--YDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKL 515
Cdd:PRK11174 392 LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 516 PHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNAD 595
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWD 551
|
330 340
....*....|....*....|....*.
gi 126927 596 VIAGFDGGVIVEQGNHDELMREKGIY 621
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAGGLF 577
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1043-1261 |
2.12e-53 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 196.80 E-value: 2.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFD 1122
Cdd:TIGR01842 326 PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIA-YGDNSRAvshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:TIGR01842 406 GTVAENIArFGENADP---EKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1202 SALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1054-1268 |
6.71e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 196.22 E-value: 6.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGD 1133
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1134 NSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQ 1213
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1214 EALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
316-617 |
2.90e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 190.64 E-value: 2.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 316 GTSLVLSNEYSIGEVLTVffSILLGTF--SIGHLAPNIEAFANARGAAFEIFKIIDNEPSidsfstkgykPDSIM----- 388
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIAG--SILVGRAlaPIDGAIGGWKQFSGARQAYKRLNELLANYPS----------RDPAMplpep 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 -GNLEFKNVHFnYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:TIGR01842 314 eGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
391-618 |
6.51e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 179.45 E-value: 6.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPV--LFATTIAENIRYGRE--DVTMDEIEKAVKEA----NAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAIAR 542
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
391-616 |
1.03e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 188.19 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 ---IGVVSQEPV--LFAT-TIAENIRYG---REDVTMDEIEKAVKEANA-----YDFIMKLPHQFdtlvgergaqlSGGQ 534
Cdd:COG1123 341 rrrVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYPHEL-----------SGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 535 KQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVE 607
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
....*....
gi 126927 608 QGNHDELMR 616
Cdd:COG1123 486 DGPTEEVFA 494
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
48-361 |
2.28e-50 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 180.06 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 48 LCMILGTLAAIihgtLLPLLmlvFGNMTDSFTKAeaSILPSITNQSGPNSTLIISNSSLeeeMAIYAYYYTgigagvliv 127
Cdd:cd18557 3 LFLLISSAAQL----LLPYL---IGRLIDTIIKG--GDLDVLNELALILLAIYLLQSVF---TFVRYYLFN--------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 128 ayiqvslwcLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGF 207
Cdd:cd18557 62 ---------IAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 208 ISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVG 287
Cdd:cd18557 133 ILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLA 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 288 IKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLgTFSIGHLAPNIEAFANARGAA 361
Cdd:cd18557 213 RKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSSLLADIMKALGAS 286
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
391-614 |
3.56e-49 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 174.29 E-value: 3.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDIRTINVR-- 463
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 YLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFIMKLPHqfdtlvgerGAQLSGGQKQ 536
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1033-1262 |
4.54e-49 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 174.06 E-value: 4.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPI--LFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1187 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
392-603 |
8.03e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 172.65 E-value: 8.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQEP--VLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 547
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGG 603
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
391-605 |
1.00e-48 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 170.86 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 551 LLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVI 605
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1037-1249 |
9.65e-48 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 168.16 E-value: 9.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1037 GVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQ 1116
Cdd:cd03246 5 NVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1117 EPILFDCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILL 1196
Cdd:cd03246 84 DDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 1197 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1249
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1050-1258 |
3.04e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 168.90 E-value: 3.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFD 1122
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYGDNSRAVS----HEEIVRAA-KEANihqfidsLPDKYNTRVgdKGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKlkeeLDERVEEAlRKAA-------LWDEVKDRL--HALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1198 DEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1034-1248 |
6.69e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 167.26 E-value: 6.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGI 1113
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKyNTRvgdkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDR-SPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1192 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1034-1249 |
1.19e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.53 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGI 1113
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQEPILFDCSIAENIAYGDNSRavsHEEIVRAAKEANIHQFidSLPDKY-NTRVgdkgTQLSGGQKQRIAIARALVRQP 1192
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLR---ERKFDRERALELLERL--GLPPDIlDKPV----ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1033-1261 |
3.99e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 174.32 E-value: 3.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPN--IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWL 1107
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1108 RAHLGIVSQEPIL-FDC--SIAENIAYG-DNSRAVSHEEIVRAAKEAnIHQ------FIDSLPDkyntrvgdkgtQLSGG 1177
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LERvglppdLADRYPH-----------ELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
....*..
gi 126927 1255 HQQLLAQ 1261
Cdd:COG1123 489 TEEVFAN 495
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
409-558 |
7.54e-46 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 162.05 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLF-ATTIAENI 487
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 488 RYGREdvtMDEIEKAVKEANAYDFI--MKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
391-609 |
8.04e-46 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 164.60 E-value: 8.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSR-SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI- 468
Cdd:cd03257 2 LEVKNLSVSFPTGgGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 --IGVVSQEPVL-------FATTIAENIRYGREDVTMDEIEKAVKEA-----NAYDFIMKLPHQfdtlvgergaqLSGGQ 534
Cdd:cd03257 82 keIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPHE-----------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 535 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
972-1232 |
1.65e-45 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 172.93 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 972 VMLVFSAvvFGAMAAgnTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEG-NVKFNGVQFNYPTRPniPV 1050
Cdd:TIGR02868 277 VLLPLAA--FEAFAA--LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN-- 1128
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlr 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDnsraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:TIGR02868 431 LARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
250 260
....*....|....*....|....
gi 126927 1209 EKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:TIGR02868 507 ADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1031-1254 |
1.80e-45 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 162.97 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1031 GNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAakeanihqfidslpdkynTRVGDKGTQLSGGQKQRIAIARALV 1189
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1190 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1035-1253 |
2.41e-45 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 161.71 E-value: 2.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1035 FNGVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGIV 1114
Cdd:cd03247 3 INNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1115 SQEPILFDCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:cd03247 81 NQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1195 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1253
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
391-586 |
3.85e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.29 E-value: 3.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENI----RYGREDVTMDEIEKAVKEANaydfimkLPHQF-DTLVGErgaqLSGGQKQRIAIARALV 545
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 126927 546 RNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
408-1275 |
3.90e-45 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 179.20 E-value: 3.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVsidgqdirtinvrYLREIIGVVSQEPVLFATTIAENI 487
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYGREDVTMDeIEKAVK----EANaydfIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PTZ00243 742 LFFDEEDAAR-LADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 564 -SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKgIYFKLvmtqtRGNEIEpGNNAYG 642
Cdd:PTZ00243 817 vGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATL-----AAELKE-NKDSKE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 643 SQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQE---------RRLSMKEAVDEDVP---------------------- 691
Cdd:PTZ00243 890 GDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDgaaldaaagRLMTREEKASGSVPwstyvaylrfcgglhaagfvla 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 692 --------------LVSFWRILNLNLSEWPYLLVGVLCAVINGCIQPV-FAIVFS------------------------- 731
Cdd:PTZ00243 970 tfavtelvtvssgvWLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVPLrFFLSYEamrrgsrnmhrdllrsvsrgtmsff 1049
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 732 ------RIVGVFSRDDDHETKRQNCNLFSLFFLVMGLIS--FVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFD 803
Cdd:PTZ00243 1050 dttplgRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSsiLVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIK 1129
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 804 DHKNS----------TGSLTTRLASDASSVKGAMGARLAVV-----TQNVANLGTGVilslvygwQLTLLLVVIIPLIVL 868
Cdd:PTZ00243 1130 SVAKSpvftlleealQGSATITAYGKAHLVMQEALRRLDVVyscsyLENVANRWLGV--------RVEFLSNIVVTVIAL 1201
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 869 GGIIEMKLLSGQalKDKKQLEISGKIATEAIENFRTIVsltreQKFETMYAQSLQVpyrnamkkahvfgitfsftQAMMY 948
Cdd:PTZ00243 1202 IGVIGTMLRATS--QEIGLVSLSLTMAMQTTATLNWLV-----RQVATVEADMNSV-------------------ERLLY 1255
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 949 FSYAacfrfgaylVAQQLMTfENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRiiektpeidsysteglkptl 1028
Cdd:PTZ00243 1256 YTDE---------VPHEDMP-ELDEEVDALERRTGMAADVTGTVVIEPASPTSAAPHPVQ-------------------- 1305
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1029 lEGNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL 1107
Cdd:PTZ00243 1306 -AGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL 1382
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1108 RAHLGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARA 1187
Cdd:PTZ00243 1383 RRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1188 LV-RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL-LAQKGIY 1265
Cdd:PTZ00243 1460 LLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIF 1539
|
970
....*....|
gi 126927 1266 FSMVQAGAKR 1275
Cdd:PTZ00243 1540 HSMVEALGRS 1549
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
391-614 |
4.83e-45 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 162.75 E-value: 4.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSR-SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI- 468
Cdd:cd03258 2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 --IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGG 533
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLEllelvgledkADAY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 534 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQGN 610
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....
gi 126927 611 HDEL 614
Cdd:cd03258 225 VEEV 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
389-609 |
1.20e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 160.66 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 GNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFATTIAENI-RYGREDvtMDEIEKAVKeanaydfimklphqfdtlVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1033-1251 |
2.42e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.59 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIKQLN----V 1104
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1105 QWLRAHLGIVSQEPILFDC-SIAENIA----YGDNSRAVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQK 1179
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1180 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
391-610 |
5.12e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 163.32 E-value: 5.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI- 468
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 --IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGG 533
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGN 610
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
391-609 |
6.14e-44 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 157.47 E-value: 6.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINvRYLREIIG 470
Cdd:cd03247 1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
391-616 |
7.17e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 167.77 E-value: 7.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LEGVVSIDGQDIRTINVRYLRE 467
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEP--VLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDtlvgERGAQLSGGQKQRIAIARA 543
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLE---AVGLERRLD----RYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1033-1253 |
9.38e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 158.45 E-value: 9.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:cd03259 76 MVFQDYALFPhLTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1253
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
391-620 |
1.96e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 159.52 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-NVRYLREII 469
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIA 541
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 542 RALVRNPKILLLDEATSALDTES-EAVVQAALD-KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG------NHDE 613
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 126927 614 LMREKGI 620
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
391-616 |
2.38e-43 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 158.43 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREII 469
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEP---------VlfATTIAENIRYGREDVTMDEIEKAVKEAN-AYDFIMKLPHQfdtlvgergaqLSGGQKQRIA 539
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPHQ-----------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 540 IARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHD 612
Cdd:COG1124 149 IARALILEPELLLLDEPTSALD----VSVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
....
gi 126927 613 ELMR 616
Cdd:COG1124 225 DLLA 228
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
53-364 |
2.68e-43 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 159.72 E-value: 2.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 53 GTLAAIIHGTLLPLLMLVFGNMTDSftkaeasilpsITNQSGPNSTliisnsSLEEEMAIYAYYYTGIGAGVLIVAYIQV 132
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDA-----------VTNHSGSGGE------EALRALNQAVLILLGVVLIGSIATFLRS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 133 SLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWK 212
Cdd:cd18780 64 WLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 213 LTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAI 292
Cdd:cd18780 144 LTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLAR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 293 TASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVF--FSILLGtFSIGHLAPNIEAFANARGAAFEI 364
Cdd:cd18780 224 ASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL-LTSFllYTLTVA-MSFAFLSSLYGDFMQAVGASVRV 295
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
391-614 |
2.91e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 157.85 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYLREI 468
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFA-TTIAENIRYGREDVT-MDEiEKAVKEANAY-------DFIMKLPHQfdtlvgergaqLSGGQKQRIA 539
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIKVKkMSK-AEAEERAMELlervglaDKADAYPAQ-----------LSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 540 IARALVRNPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
391-609 |
7.55e-43 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 155.76 E-value: 7.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIG 470
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT-TIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 547
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEGLLNRYP----HELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 609
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
391-616 |
8.33e-43 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 156.68 E-value: 8.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:COG1127 6 IEVRNLTK---SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 -IGVVSQEPVLF-ATTIAENIRYG-RE--DVTMDEIEKAVkeanaydfIMKLphqfdTLVGERGA------QLSGGQKQR 537
Cdd:COG1127 83 rIGMLFQGGALFdSLTVFENVAFPlREhtDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 126927 615 MR 616
Cdd:COG1127 230 LA 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
391-617 |
1.05e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.99 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlREIIG 470
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRN 547
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1042-1253 |
1.06e-42 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 155.74 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1042 YPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RAHLGIVSQE 1117
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1118 PI-----LFdcSIAENIA-----YGDNSRAvshEEIVRAAKEANIH-----QFIDSLPDkyntrvgdkgtQLSGGQKQRI 1182
Cdd:cd03257 91 PMsslnpRM--TIGEQIAeplriHGKLSKK---EARKEAVLLLLVGvglpeEVLNRYPH-----------ELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1183 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1051-1202 |
1.21e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 152.80 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILF-DCSIAENI 1129
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1130 AYGDNSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEA-LEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
97-361 |
1.72e-42 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 157.32 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 97 STLIISNSSleEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTD 176
Cdd:cd18572 24 DAVVADGSR--EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 177 DVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSS---ALWAKVLtsftNKELQ-AYAKAGAV 252
Cdd:cd18572 102 DCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITkvyGRYYRKL----SKEIQdALAEANQV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 253 AEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT 332
Cdd:cd18572 178 AEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVT 257
|
250 260 270
....*....|....*....|....*....|
gi 126927 333 -VFFSILLGTfSIGHLAPNIEAFANARGAA 361
Cdd:cd18572 258 fMLYQQQLGE-AFQSLGDVFSSLMQAVGAA 286
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
391-605 |
2.26e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 154.57 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REIIGVVSQEPVLFAT-TIAENIRYGredVTMDEIEKAVKEANAYDFI--MKLPHQFDTLVgergAQLSGGQKQRIAIAR 542
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 543 ALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVIAGFDGGVI 605
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
408-1265 |
2.77e-42 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 169.71 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtinvrylreiIGVVSQEPVLFATTIAENI 487
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYGredVTMDEIE--KAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD--TE 563
Cdd:TIGR01271 508 IFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 564 SEaVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIY---------------------- 621
Cdd:TIGR01271 585 KE-IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdnfsaerrnsil 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 622 ---------------------------------------------------FKLV---MTQTRGNEI-----EPGNNAYG 642
Cdd:TIGR01271 664 tetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVqmgPQKAQATTIedavrEPSERKFS 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 643 SQSDTDASE-------------------------LTSEESKSPLIRRSIYRSVHRK----QDQE---------RRLS--- 681
Cdd:TIGR01271 744 LVPEDEQGEeslprgnqyhhglqhqaqrrqsvlqLMTHSNRGENRREQLQTSFRKKssitQQNElaseldiysRRLSkds 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 682 ---MKEAVDED------------VPLVSFW----RILNLNLSewpYLLVGVLCAVIngciqpVFAIVFSRIVGVF----- 737
Cdd:TIGR01271 824 vyeISEEINEEdlkecfaderenVFETTTWntylRYITTNRN---LVFVLIFCLVI------FLAEVAASLLGLWlitdn 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 738 -----SRDDDHETKRQNCNLFS----------LFFLVMGLI-SFVTY-FFQGFTFGKAGEILTKRVRYMVFKSMLRQDIS 800
Cdd:TIGR01271 895 psapnYVDQQHANASSPDVQKPviitptsayyIFYIYVGTAdSVLALgFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMA 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 801 WFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQ-NVANLGTGVILSLVYGWqltlLLVVIIPLIVLGGIIEMKLL-S 878
Cdd:TIGR01271 975 VLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQlTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAYFLrT 1048
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 879 GQALKdkkQLEISGK--IATEAIENFR---TIVSLTREQKFETMYAQSLQvpyrnamkkahvfgitfsfTQAMMYFSYAA 953
Cdd:TIGR01271 1049 SQQLK---QLESEARspIFSHLITSLKglwTIRAFGRQSYFETLFHKALN-------------------LHTANWFLYLS 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 954 CFRFGAYLVAqqlMTFenvMLVFSAVVFGAMAAGN----------------TSSF------APDYAKAKVSASHIIRIIE 1011
Cdd:TIGR01271 1107 TLRWFQMRID---IIF---VFFFIAVTFIAIGTNQdgegevgiiltlamniLSTLqwavnsSIDVDGLMRSVSRVFKFID 1180
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1012 KTPEiDSYSTEGLKPTLL-----------------EGNVKFNGVQFNYpTRPNIPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:TIGR01271 1181 LPQE-EPRPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGK 1258
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1075 STVVQLLERFYDpMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAAKEANIHQ 1154
Cdd:TIGR01271 1259 STLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKS 1334
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1155 FIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1234
Cdd:TIGR01271 1335 VIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEA 1414
|
1050 1060 1070
....*....|....*....|....*....|.
gi 126927 1235 IQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR01271 1415 LLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1033-1261 |
3.20e-42 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 154.66 E-value: 3.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVFLDGKEIKQLN---VQ 1105
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1106 WLRAHLGIVSQEPILFDC-SIAENIAYGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPdkyntrvgdkgTQLSGGQKQ 1180
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQ 1257
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....
gi 126927 1258 LLAQ 1261
Cdd:cd03258 228 VFAN 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
50-361 |
3.72e-42 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 156.56 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAeasilpsitnqsGPNSTLIIsnssleeemaiYAYYYTGIGAGVLIVAY 129
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPA------------GDLSLLLW-----------IALLLLLLALLRALLSY 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:cd07346 58 LRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:cd07346 138 NWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFSiLLGTFS--IGHLAPNIEAFANARGAA 361
Cdd:cd07346 218 AARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE-LVAFLA-YLGMLFgpIQRLANLYNQLQQALASL 289
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
391-608 |
5.30e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.66 E-value: 5.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPS-RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REIIGVVSQEPVLFAT-TIAENI----RYGREDVtmDEIEKAVKEANAY----DFIMKLPHQfdtlvgergaqLSGGQKQ 536
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENValplLLAGVSR--KERRERARELLERvglgDRLDHRPSQ-----------LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFDGGVIVEQ 608
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
391-616 |
5.31e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 154.38 E-value: 5.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFA-TTIAENI-------RYGREdvtmdEIEKAVKEANAydfIMKLPHQfdTLVGERGAQLSGGQKQRIAIAR 542
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPKE-----KIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
391-586 |
6.24e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.86 E-value: 6.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylreiI 469
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFA-TTIAENIRYGREDVTMDEiEKAVKEANAY-------DFIMKLPHQfdtlvgergaqLSGGQKQRIAIA 541
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPK-AERRERARELlelvglaGFEDAYPHQ-----------LSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126927 542 RALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
391-617 |
7.22e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 156.37 E-value: 7.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL---EGVVSIDGQDIRTINVRYLR 466
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 EI----IGVVSQEPvlFA---------TTIAENIRYgREDVTMDEIEKAVKEA-------NAYDFIMKLPHQFdtlvger 526
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPHEL------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 527 gaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAG 599
Cdd:COG0444 152 ----SGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*...
gi 126927 600 FDGGVIVEQGNHDELMRE 617
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
391-617 |
8.55e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 154.05 E-value: 8.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVL-FATTIAENIRYGR------------EDvtMDEIEKAVKEANAYDFIMKLphqFDTlvgergaqLSGGQKQR 537
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrpsaED--REAVEEALERTGLEHLADRP---VDE--------LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
...
gi 126927 615 MRE 617
Cdd:COG1120 226 LTP 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
391-586 |
1.21e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 152.63 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylreiI 469
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFA-TTIAENIRYGRE--DVTMDEIEKAVKEANA----YDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 542
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLElvglSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
391-616 |
1.33e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 153.04 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 -IGVVSQEPVLF-ATTIAENIRYG-REDVTMDE--IEKAVKeanaydfiMKLphqfdTLVGERG------AQLSGGQKQR 537
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLSEeeIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 538 IAIARALVRNPKILLLDEATSALD-TESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 126927 615 MR 616
Cdd:cd03261 225 RA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1033-1251 |
1.79e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 151.86 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAHL 1111
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEAnIHQ-----FIDSLPDkyntrvgdkgtQLSGGQKQRIAIA 1185
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-LELvglsgFENAYPH-----------QLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1186 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIEN--GKVKE 1251
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1049-1261 |
3.46e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 151.69 E-value: 3.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILF-D 1122
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYGD-NSRAVSHEEIVRAAKEAnihqfidsLpdkynTRVG--DKG----TQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:COG1126 92 LTVLENVTLAPiKVKKMSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1196 LLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG1126 159 LFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1047-1261 |
5.18e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.37 E-value: 5.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAHLGIVSQEPILF-DCSI 1125
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 AENIAYGDNSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1206 TESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG1131 164 PEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1033-1254 |
5.24e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.26 E-value: 5.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:COG3842 6 LELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIENGKVKEHGT 1254
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1033-1261 |
8.54e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.53 E-value: 8.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:COG1123 5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPI--LFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIA 1183
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 126927 1261 Q 1261
Cdd:COG1123 233 A 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1042-1260 |
1.04e-40 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 150.72 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1042 YPTRP-NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL 1120
Cdd:COG1124 11 YGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1121 -------FDCSIAE--NIAYGDNSRavshEEIVRAAKEANIH-QFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVR 1190
Cdd:COG1124 91 slhprhtVDRILAEplRIHGLPDRE----ERIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1191 QPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG1124 156 EPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
115-624 |
1.09e-40 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 164.73 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 115 YYYTGIGAGVLIVAY-IQVSLWCLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:TIGR00957 1011 YGALGILQGFAVFGYsMAVSIGGIQASRVLH---QDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWakVLTSFTNKELQAYAKAGAVAE--EVLAAIRTVIAFGGQQK 271
Cdd:TIGR00957 1088 GSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFY--VASSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQER 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 272 ELERYNKNLEEAKnvgikKAITASI------SIGIAYL-----LVYASYALAFWYGTS--LV-LSNEYSIGevLTVFFSI 337
Cdd:TIGR00957 1166 FIHQSDLKVDENQ-----KAYYPSIvanrwlAVRLECVgncivLFAALFAVISRHSLSagLVgLSVSYSLQ--VTFYLNW 1238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 338 LLGTFSigHLAPNIeafanargAAFEIFKIIDNEPSIDSFSTKGYKPDSI---MGNLEFKNVHFNYpsRSEVQ-ILKGLN 413
Cdd:TIGR00957 1239 LVRMSS--EMETNI--------VAVERLKEYSETEKEAPWQIQETAPPSGwppRGRVEFRNYCLRY--REDLDlVLRHIN 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 414 LKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI----RY 489
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQY 1386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 490 GREDVTMdeiekAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQ 569
Cdd:TIGR00957 1387 SDEEVWW-----ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 570 AALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:TIGR00957 1462 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
391-605 |
1.73e-40 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 148.83 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYLREI 468
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFA-TTIAENIRYGRedVTMDEIEKAVKEANAYDFIMK--LPHQFDtlvgERGAQLSGGQKQRIAIARALV 545
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 546 RNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 605
Cdd:cd03262 152 MNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
391-603 |
2.00e-40 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 147.33 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT--INVRYLREI 468
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFAT-TIAENIRYGredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRN 547
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 548 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFDGG 603
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1033-1259 |
3.57e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 149.42 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPIL-FDCSIAENIAYG-----DNSRAVSHE--EIVRAA-KEANIHQFIDslpdkynTRVgdkgTQLSGGQKQRIA 1183
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlGLFGRPSAEdrEAVEEAlERTGLEHLAD-------RPV----DELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1033-1251 |
3.60e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAHL 1111
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1187 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIEN--GKVKE 1251
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
392-603 |
4.67e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.47 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 552 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFDGG 603
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1033-1248 |
6.16e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 146.85 E-value: 6.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNI--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGSVFLDGKeikqlnvqwlr 1108
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1109 ahLGIVSQEPILFDCSIAENIAYG---DNSRavsHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 1185
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFGkpfDEER---YEKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1186 RALVRQPHILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIENGK 1248
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1033-1262 |
8.66e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 148.73 E-value: 8.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-QLNVQWLRAHL 1111
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVSQEPilfD----CSIAEN-IAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRI 1182
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1183 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 126927 1261 QK 1262
Cdd:TIGR04520 226 QV 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-614 |
9.69e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.26 E-value: 9.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD--P---LEGVVSIDGQDI--RTINVR 463
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 YLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFImKlphqfDTLvGERGAQLSGGQKQ 536
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEV-K-----DRL-KKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGFDGGVIVEQG 609
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235
|
....*
gi 126927 610 NHDEL 614
Cdd:COG1117 236 PTEQI 240
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1033-1249 |
1.08e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 146.87 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---- 1107
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1108 RAHLGIVSQE----PILfdcSIAENIAYGDNSRAVSHEEIVRAAKEAnihqfIDS--LPDKYNTRVGdkgtQLSGGQKQR 1181
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1182 IAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIENGKV 1249
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1033-1254 |
1.78e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 150.23 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVFLDGKEIKQLNVQWLR 1108
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1109 A---HLGIVSQEPILFD-CSIAENIAY-----GdnsraVSHEEIvrAAKeanihqfIDSLPDkyntRVG--DKG----TQ 1173
Cdd:COG1135 79 AarrKIGMIFQHFNLLSsRTVAENVALpleiaG-----VPKAEI--RKR-------VAELLE----LVGlsDKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVK 1250
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....
gi 126927 1251 EHGT 1254
Cdd:COG1135 221 EQGP 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
61-641 |
2.19e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 160.14 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 61 GTLLPLLMLVFGNMTDSFTKAEASILPSITNQSGPNSTliisnssleeEMAIYAYYYTGIGAGVLIVAYIQvSLW----C 136
Cdd:PLN03232 910 GLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSY----------SPGFYIVVYALLGFGQVAVTFTN-SFWlissS 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 137 LAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGF-IIGFISgwklTL 215
Cdd:PLN03232 979 LHAAKRLH---DAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFaLIGTVS----TI 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 216 VILAVSPLIGL---------SSALWAKVLTSFTNKELqaYAKAGAvAEEVLAAIRTVIAFGGQQKELERYNKNleeakNV 286
Cdd:PLN03232 1052 SLWAIMPLLILfyaaylyyqSTSREVRRLDSVTRSPI--YAQFGE-ALNGLSSIRAYKAYDRMAKINGKSMDN-----NI 1123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 287 GIKKAITAS--------ISIGIAYLLVYASYALaFWYGTSlvlSNEYSIGEVLTVFFS-------ILLGTFSIGHLAPN- 350
Cdd:PLN03232 1124 RFTLANTSSnrwltirlETLGGVMIWLTATFAV-LRNGNA---ENQAGFASTMGLLLSytlnittLLSGVLRQASKAENs 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 351 ---IEAFANARGAAFEIFKIIDNEPSIDSFSTKGykpdsimgNLEFKNVHFNYpsRSEVQ-ILKGLNLKVKSGQTVALVG 426
Cdd:PLN03232 1200 lnsVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVG 1269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 427 NSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDeIEKAVKEA 506
Cdd:PLN03232 1270 RTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD-LWEALERA 1348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 507 NAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 586
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 587 RLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKlvMTQTRGneiePGNNAY 641
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFR--MVHSTG----PANAQY 1478
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
388-609 |
6.19e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.09 E-value: 6.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLRE 467
Cdd:COG3842 3 MPALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IiGVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARAL 544
Cdd:COG3842 79 V-GMVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQG 609
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1033-1260 |
7.16e-39 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 145.14 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKEanIHQFIDSLPDKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADE--LLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1192 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1264 |
9.28e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 145.90 E-value: 9.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPilfD-----CSIAENIAYGDNSRAVSHEE----IVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIA 1183
Cdd:PRK13632 87 IIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
...
gi 126927 1262 KGI 1264
Cdd:PRK13632 233 KEI 235
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
102-334 |
9.67e-39 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 146.51 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 102 SNSSLEEEMAIYAYYYTGIGAGVLIVA----YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDD 177
Cdd:cd18573 28 KESGDIEIFGLSLKTFALALLGVFVVGaaanFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 178 VSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVL 257
Cdd:cd18573 108 TSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 258 AAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVF 334
Cdd:cd18573 188 SNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGD-LTSF 263
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
392-620 |
1.02e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 145.90 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:PRK13632 9 KVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQEP---VLFATT---IA---ENIRYGREDVTmDEIEKAVKEANAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAIAR 542
Cdd:PRK13632 88 IFQNPdnqFIGATVeddIAfglENKKVPPKKMK-DIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGI 620
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
391-619 |
1.83e-38 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 144.23 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIiG 470
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEanaYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRN 547
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 548 PKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:COG4555 151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1044-1248 |
1.99e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 141.56 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN--VQWLRAHLGIVSQEPILF 1121
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 -DCSIAENIAYGdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1201 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1034-1248 |
2.00e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 140.84 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGI 1113
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQepilfdcsiaeniaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPH 1193
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1194 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGK 1248
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1050-1258 |
2.37e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 144.41 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFD 1122
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYG-----DNSRAVsHEEIVRAA-KEANihqfidsLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1197 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIENGKVKEHGTHQQL 1258
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1049-1260 |
2.91e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 143.58 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV---QWLRAHLGIVSQEPILFDC-S 1124
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAYG-DNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1200 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1036-1261 |
4.15e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.39 E-value: 4.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1036 NGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVS 1115
Cdd:PRK13635 9 EHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1116 QEPilfD-----CSIAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 1186
Cdd:PRK13635 88 QNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1187 ALVRQPHILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
388-561 |
1.32e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 145.22 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlRE 467
Cdd:COG3839 1 MASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IiGVVSQEPVLF-ATTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARAL 544
Cdd:COG3839 77 I-AMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGLEDLLDRKP----KQLSGGQRQRVALGRAL 148
|
170
....*....|....*..
gi 126927 545 VRNPKILLLDEATSALD 561
Cdd:COG3839 149 VREPKVFLLDEPLSNLD 165
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1033-1260 |
1.40e-37 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 141.49 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV---QWLRA 1109
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILFDC-SIAENIAYGDNS-RAVSHEEIVRAAKE----ANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIA 1183
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREhTRLSEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1184 IARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1034-1263 |
2.11e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 141.15 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvQWLRAHLGI 1113
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEAnIHQFIdsLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 1192
Cdd:COG4555 79 LPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1049-1271 |
2.22e-37 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 141.58 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IaygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1209 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK-GIYFSMVQA 1271
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
391-607 |
2.35e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLRE 467
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQE-PVLFATTIAENIRY-----GREDvtmDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQR 537
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREVldlvGLSDKAKALPHE-----------LSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFDGGVIVE 607
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1055-1261 |
6.21e-37 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 140.47 E-value: 6.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA----HLGIVSQEPILF-DCSIAENI 1129
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 AYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1206 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
406-617 |
1.55e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.41 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI---IGVVSQEPvlFA-- 480
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--YAsl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 -------TTIAENIRYgREDVTMDEIEKAVKEA------NAyDFIMKLPHQFdtlvgergaqlSGGQKQRIAIARALVRN 547
Cdd:COG4608 109 nprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 548 PKILLLDEATSALDteseaV-VQAA-----LD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG4608 176 PKLIVCDEPVSALD-----VsIQAQvlnllEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-617 |
2.90e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylreiIG 470
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVL---FATTIAENI------------RYGREDVtmDEIEKAVKEANAYDFImklphqfDTLVGErgaqLSGGQK 535
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRADR--EAVDEALERVGLEDLA-------DRPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFDGGVIVEqGNHDE 613
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEE 224
|
....
gi 126927 614 LMRE 617
Cdd:COG1121 225 VLTP 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
392-609 |
3.60e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 140.71 E-value: 3.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:PRK11153 3 ELKNISKVFPQGGrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 -IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGGQ 534
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 535 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
113-664 |
6.87e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 149.12 E-value: 6.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 113 YAYYYTGIGAGVLIVAYIQvSLW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDK 188
Cdd:PLN03130 955 YNLIYALLSFGQVLVTLLN-SYWlimsSLYAAKRLH---DAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVF 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 189 IGMFFQSITTFLAGFI-IGFISgwklTLVILAVSPLIGL---------SSALWAKVLTSFTNKELqaYAKAGAvAEEVLA 258
Cdd:PLN03130 1031 VNMFLGQIFQLLSTFVlIGIVS----TISLWAIMPLLVLfygaylyyqSTAREVKRLDSITRSPV--YAQFGE-ALNGLS 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 259 AIRTVIAF-------GGQQKELERYN-KNLEEAKNVGIKKAITASISIGI-AYLLVY----ASYALAFWYGTSLVLSNEY 325
Cdd:PLN03130 1104 TIRAYKAYdrmaeinGRSMDNNIRFTlVNMSSNRWLAIRLETLGGLMIWLtASFAVMqngrAENQAAFASTMGLLLSYAL 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 326 SIGEVLTvffsillGTFSIGHLAPN----IEAFANARGAAFEIFKII-DNEPSidsfstKGYkPDSimGNLEFKNVHFNY 400
Cdd:PLN03130 1184 NITSLLT-------AVLRLASLAENslnaVERVGTYIDLPSEAPLVIeNNRPP------PGW-PSS--GSIKFEDVVLRY 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 401 psRSEVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLF 479
Cdd:PLN03130 1248 --RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF 1325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 480 ATTIAENIRYGREDVTMDEIEkAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PLN03130 1326 SGTVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 560 LDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKlVMTQTRGneiePGNN 639
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS-KMVQSTG----AANA 1479
|
570 580
....*....|....*....|....*...
gi 126927 640 AYgSQS---DTDASELTSEESKSPLIRR 664
Cdd:PLN03130 1480 QY-LRSlvfGGDEDRLAREESKALDGQR 1506
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1033-1253 |
7.98e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.95 E-value: 7.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1109
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQE-PILFDCSIAENIAY-----GdnsraVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQK 1179
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1180 QRIAIARALVRQPHILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIENGKVKEHG 1253
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
391-605 |
9.78e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 133.68 E-value: 9.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT-TIAENIRYgredvtmdeiekavkeanaydfimklphqfdtlvgergaqlSGGQKQRIAIARALVRNPK 549
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 550 ILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 605
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
391-597 |
1.90e-35 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 134.13 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQ--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLyDPLEGVVSIDGQdirtinvrylre 467
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 iIGVVSQEPVLFATTIAENIRYGREdvtMDEIE-KAVKEANA--YDFIMkLPHQFDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:cd03250 68 -IAYVSQEPWIQNGTIRENILFGKP---FDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 545 VRNPKILLLDEATSALDTESEA-----VVQAALdkaREGRTTIVIAHRLSTVRNADVI 597
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQI 197
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1050-1259 |
4.33e-35 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 134.00 E-value: 4.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 1209 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
709-1004 |
4.72e-35 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 135.77 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVIngciQPVFaivFSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFqgftFGKAGEILTKRVRY 788
Cdd:cd18557 5 LLISSAAQLL----LPYL---IGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYL----FNIAGERIVARLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 789 MVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18557 74 DLFSSLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 869 GGII---EMKLLSGQALkdkKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQA 945
Cdd:cd18557 152 ASKIygrYIRKLSKEVQ---DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 946 MMYFSYAACFRFGAYLVAQ------QLMTFenvmLVFSAVVfgAMAAGNTSSFAPDYAKAkVSAS 1004
Cdd:cd18557 229 LIYLSLLLVLWYGGYLVLSgqltvgELTSF----ILYTIMV--ASSVGGLSSLLADIMKA-LGAS 286
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1033-1249 |
5.41e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.41 E-value: 5.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1109
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILFD-CSIAENI---AYGDNS------RAVSHEEIVRAakeaniHQFIDS--LPDKYNTRVGdkgtQLSGG 1177
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1036-1261 |
6.28e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.20 E-value: 6.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1036 NGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIK-QLNVQwlRAHL 1111
Cdd:COG1118 6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--ERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 1186
Cdd:COG1118 78 GFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1187 ALVRQPHILLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIENGKVKEHGTHQ 1256
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPD 219
|
....*
gi 126927 1257 QLLAQ 1261
Cdd:COG1118 220 EVYDR 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
391-614 |
8.48e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 133.46 E-value: 8.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 -IGVVSQEPVLFA-TTIAENIRYGREDVT---------MDEIEKAvkeaNAYDFIMKLphQFDTLVGERGAQLSGGQKQR 537
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQ----RALAALERV--GLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 538 IAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVR-NADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
391-606 |
1.19e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 133.26 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 -IGVVSQEPVLFA-TTIAENI-----------RYGREDVTMDEIEKAvkeanaydfimklphqFDTL--VG------ERG 527
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 528 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGV 604
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
gi 126927 605 IV 606
Cdd:COG3638 225 VV 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
413-617 |
1.29e-34 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 133.92 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 413 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTIAENI 487
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYGREDVTMDEIEKAVKEANAY------DFIMKLPHqfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 562 TESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1050-1249 |
1.40e-34 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 131.88 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW--LRAHLGIVSQEPILF-DCSIA 1126
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYGD-NSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:cd03262 95 ENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 126927 1202 SALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03262 164 SALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
408-627 |
1.75e-34 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 133.11 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI 487
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 567
Cdd:cd03288 116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 568 VQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKLVMT 627
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
122-361 |
2.75e-34 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 133.76 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 122 AGVLIV----AYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSIT 197
Cdd:cd18576 43 LGLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 198 TFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYN 277
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 278 KNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLGTfSIGHLAPNIEAFAN 356
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQK 281
|
....*
gi 126927 357 ARGAA 361
Cdd:cd18576 282 ALGAS 286
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1033-1261 |
3.60e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAHLG 1112
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQE-------PIlfdcSIAENIAYG--------DNSRAVSHEEIVRAAKEANIHQFIDslpdkynTRVGdkgtQLSGG 1177
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGrygrrglfRRPSRADREAVDEALERVGLEDLAD-------RPIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIeNGKVKEHGTH 1255
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 126927 1256 QQLLAQ 1261
Cdd:COG1121 223 EEVLTP 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1049-1258 |
4.68e-34 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 131.21 E-value: 4.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIkqLNVQWLRAHLGIVSQEPILF-DCSIAE 1127
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDNSRAVSHEEIVRAAKEAnIHQF-IDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEA-LDLVqLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1207 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03300 164 KLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
391-615 |
5.19e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 131.37 E-value: 5.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNV--HFnypsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIR--TINVRYLR 466
Cdd:PRK09493 2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 EIIGVVSQEPVLFATTIA-ENIRYGREDVTmdEIEKAVKEANAYDFIMKlphqfdtlVG--ERG----AQLSGGQKQRIA 539
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGPLRVR--GASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 540 IARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
709-1006 |
9.41e-34 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 132.29 E-value: 9.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrqnCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL----LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 789 MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd07346 77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 869 GGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMY 948
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 949 FSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHI 1006
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1033-1261 |
1.11e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 131.39 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 1186
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1187 ALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1033-1249 |
1.44e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 127.51 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLG 1112
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILF-DCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1192 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
391-585 |
1.92e-33 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 128.68 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI---RTINVRYLRE 467
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLvgerGAQLSGGQKQRIAIARAL 544
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA 585
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
392-605 |
1.98e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 128.42 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtiNVRYLREIIGV 471
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQEPVL---FATTIAENI------------RYGREDvtMDEIEKAVKEANAYDFIMKlphQFDtlvgergaQLSGGQKQ 536
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKAD--KAKVDEALERVGLSELADR---QIG--------ELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVI 605
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1049-1254 |
2.83e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.15 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAE 1127
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEAlrmvQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1204 LDTESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:PRK09452 175 LDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1034-1249 |
2.94e-33 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 129.22 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RAH 1110
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1111 LGIVSQEPILFD-CSIAENI---AYGDNS------RAVSHEEIVRAAkeANIHQFidSLPDKYNTRVGdkgtQLSGGQKQ 1180
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVlsgRLGRRStwrslfGLFPKEEKQRAL--AALERV--GLLDKAYQRAD----QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-616 |
4.35e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 135.97 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSR--------SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLyDPLEGVVSIDGQDIRTIN- 461
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 --VRYLREIIGVVSQEPvlFAT-----TIAENIRYG----REDVTMDEIEKAVKEA-----------NAYdfimklPHQF 519
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 520 dtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN 593
Cdd:COG4172 427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....
gi 126927 594 -ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1042-1261 |
4.89e-33 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 130.94 E-value: 4.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1042 YPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVFLDGKEIKQLNVQWLRA----HLGI 1113
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQEP---------ILFdcSIAENI-AYGDNSRAVSHEEIVRAAKEANIH---QFIDSLPdkyntrvgdkgTQLSGGQKQ 1180
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPdpeRRLDRYP-----------HELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1181 RIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233
|
....*...
gi 126927 1254 THQQLLAQ 1261
Cdd:COG0444 234 PVEELFEN 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
392-609 |
5.13e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.40 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQepvlfattiaenirygredvtmdeiekAVKEANAYDFIMKlphQFDTlvgergaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 552 LLDEATSALDTESE-AVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 609
Cdd:cd03214 120 LLDEPTSHLDIAHQiELLELLRRLARErGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1033-1254 |
5.44e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.73 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:COG3839 79 MVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKPK-----------QLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1188 LVRQPHILLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIENGKVKEHGT 1254
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
391-597 |
7.72e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 126.82 E-value: 7.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlREIIG 470
Cdd:COG4133 3 LEAENLSC---RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT-TIAENIR-----YGReDVTMDEIEKAVKEanaydfiMKLPHQFDTLVGergaQLSGGQKQRIAIARAL 544
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVI 597
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1048-1260 |
2.03e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 126.01 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPILF-DCS 1124
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAYGDNSRAvsheeivRAAKEANIHQFIDSLPDKYnTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1205 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIENGKVKEHGTHQQLLA 1260
Cdd:cd03224 164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
391-616 |
2.15e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.88 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT-INVRYLReiI 469
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKE----------ANAYdfimklPHQfdtlvgergaqLSGGQKQ 536
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------PSQ-----------LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 537 RIAIARALVRNPKILLLDEATSALDT----ESEAVVQAALDkaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNH 611
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTP 218
|
....*
gi 126927 612 DELMR 616
Cdd:COG1118 219 DEVYD 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
394-586 |
2.17e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 125.45 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 394 KNVHFNYPSRSEvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIrtiNVRYLREIIGVVS 473
Cdd:cd03226 3 ENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 474 QEP--VLFATTIAENIRYGREDVTMD--EIEKAVKEANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIARALVRNPK 549
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 126927 550 ILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAH 586
Cdd:cd03226 147 LLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-616 |
2.18e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.82 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13635 6 IRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEP--VLFATTIAENIRYGRED--VTMDE----IEKAVKEANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 542
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
391-618 |
3.27e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.12 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYL--REI 468
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEP--VLFATTIAENIRYGREDV--TMDEIEKAVKEA----NAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAI 540
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 541 ARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1055-1261 |
3.76e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.64 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAhLGIVSQEPILFD-CSIAENIAYGD 1133
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP-VSMLFQENNLFPhLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1134 NSR----AVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1205
Cdd:COG3840 97 RPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1206 TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG3840 166 QEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1045-1250 |
4.93e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 124.29 E-value: 4.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlnvQWLRAHLGIVSQEP--ILFD 1122
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVdyQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:cd03226 87 DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 126927 1203 ALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK 1250
Cdd:cd03226 156 GLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
391-614 |
1.28e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.89 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDI---RTINV 462
Cdd:PRK14239 6 LQVSDLSVYY---NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 463 RyLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDE-IEKAVKEANAYDFIMKLPHqfDTLVGergaqLSGGQK 535
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKDRLH--DSALG-----LSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1026-1261 |
1.38e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 131.35 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1026 PTLLEGNvkfnGVQFNYPTRPNI--------PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGSVFLDGK 1097
Cdd:COG4172 273 PPLLEAR----DLKVWFPIKRGLfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1098 EIKQLN---VQWLRAHLGIVSQEPilFDC-----SIAENIAYGdnsRAVSHEEIVRAAKEANIhqfIDSLpdkynTRVG- 1168
Cdd:COG4172 348 DLDGLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGl 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1169 DKGT------QLSGGQKQRIAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQ 1236
Cdd:COG4172 415 DPAArhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVR 490
|
250 260
....*....|....*....|....*.
gi 126927 1237 N-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4172 491 AlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1044-1243 |
1.43e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.97 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAHLGIVSQEPILF-D 1122
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIA-----YGdnsRAVSHEEIVRAAKEANIHQFIDslpdkynTRVGdkgtQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126927 1198 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1243
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1036-1253 |
1.60e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 121.77 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1036 NGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVS 1115
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1116 QepilfdcsiaeniaygdnsravsheeivrAAKEANIHQFIDSLpdkYNTrvgdkgtqLSGGQKQRIAIARALVRQPHIL 1195
Cdd:cd03214 80 Q-----------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1196 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1253
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1033-1254 |
2.40e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.45 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGSVFLDGKEIKQLNVQWLR 1108
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1109 A---HLGIVSQE-PILFDCSIAENIAYGdnsravshEEIVRAAKeANIHQFIDSLPDkyntRVG--DKG----TQLSGGQ 1178
Cdd:PRK11153 79 KarrQIGMIFQHfNLLSSRTVFDNVALP--------LELAGTPK-AEIKARVTELLE----LVGlsDKAdrypAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1179 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGT 1254
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1046-1258 |
2.65e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 123.22 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCS 1124
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAYGDNSRAVShEEIVRAAKEANIHQFI-----DSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:cd03296 91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1200 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1046-1249 |
2.87e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAHLGIVSQEPILF-DC 1123
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYGD---NSRAVSHEEIVRAAKEA----NIHqfIDslPDkynTRVGDkgtqLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlGLD--ID--PD---TPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1197 LDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG1129 164 LDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1033-1249 |
3.16e-31 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 122.52 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1109
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQE-PILFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAI 1184
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIENGKV 1249
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1034-1253 |
3.25e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 122.26 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAHLGI 1113
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQEPIL---FDCSIAENIAYGDNSRAVSHEEIVRAAKEAnIHQFIDS--LPDKYNTRVGdkgtQLSGGQKQRIAIARAL 1188
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK-VDEALERvgLSELADRQIG----ELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1189 VRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIeNGKVKEHG 1253
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
391-617 |
6.41e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 121.77 E-value: 6.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY-LREII 469
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAVKEAnaYDFIMKLphqfDTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRL----KERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 549 KILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:cd03224 152 KLLLLDEPSEGL---APKIVEeifEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
409-613 |
7.29e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 122.06 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENI 487
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYGREDVTMD--EIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 565
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLEIAE---MLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 566 AVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 613
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
391-614 |
7.78e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 123.28 E-value: 7.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIAR 542
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1042-1258 |
1.09e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 121.07 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1042 YPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILF 1121
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 D-CSIAENIAYGDNSRAVSHEEIvraakEANIHQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:cd03263 88 DeLTVREHLRFYARLKGLPKSEI-----KEEVELLLRvlGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1199 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1050-1254 |
1.16e-30 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 121.39 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGIVS--QEPILF-DCSIA 1126
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENI---AYGDNSRAVSHEEIVRAAKEAN--IHQFIDS--LPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:cd03219 94 ENVmvaAQARTGSGLLLARARREEREARerAEELLERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1200 ATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:cd03219 170 PAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1051-1258 |
1.31e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 124.07 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQEP--------- 1118
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnprmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ---IlfdcsIAENIAYgdnsravsHEEIVRAAKEANIHQFIDslpdkyntRVGDKGT-------QLSGGQKQRIAIARAL 1188
Cdd:COG4608 114 vgdI-----IAEPLRI--------HGLASKAERRERVAELLE--------LVGLRPEhadryphEFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1189 VRQPHILLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:COG4608 173 ALNPKLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
391-609 |
1.52e-30 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 120.44 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRtiNVRYLREIIG 470
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQIEH----LLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
407-614 |
1.69e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 121.40 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVV-----SIDGQdiRTIN-----VRYLREIIGVVSQEP 476
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 477 VLFA-TTIAENIRYGreDVTMDEIEKAVKEANAYDFIMKLphqfdTLVGERGA---QLSGGQKQRIAIARALVRNPKILL 552
Cdd:PRK11264 95 NLFPhRTVLENIIEG--PVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 553 LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
388-595 |
2.12e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGN-LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLR 466
Cdd:PRK13650 1 MSNiIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 EIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPhqfdtlvgergAQLSGGQKQRI 538
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNAD 595
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSD 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1258 |
2.15e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.78 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPI-LFDCSIAE-NIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1187 ALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
391-617 |
3.19e-30 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 120.03 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIrtINVRYLREIIG 470
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEAnaydfiMKLPhQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
391-609 |
4.44e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 120.53 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLEGVVSIDG------QDI--RTINV 462
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 463 RYLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQK 535
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFDG-----GVIVE 607
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVE 236
|
..
gi 126927 608 QG 609
Cdd:PRK14258 237 FG 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1051-1269 |
5.42e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.61 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP--ILFDCSIAEN 1128
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1205 DTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG-----THQQLLAQKGIYFSMV 1269
Cdd:PRK13647 170 DPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLV 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1044-1246 |
1.18e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.58 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPIL 1120
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1121 FD-CSIAENIAYG---DNSRAVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 126927 1197 LDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIEN 1246
Cdd:COG4136 157 LDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1051-1249 |
1.29e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 117.78 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-D 1122
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYG-----DNSRAVSHEEIVRAAKeanihqfIDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1198 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
391-561 |
1.32e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.36 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI-------RTINVr 463
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 ylreiigvVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEAnaydfiMKLPhQFDTLVGERGAQLSGGQKQRIAI 540
Cdd:PRK09452 91 --------VFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMV-QLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 126927 541 ARALVRNPKILLLDEATSALD 561
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
391-618 |
1.74e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.07 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13647 5 IEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAIAR 542
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
403-608 |
3.36e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 117.98 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLREIIGVVSQE---P 476
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 477 VLFATTIAENIRYGREDVT-MDEIEKAVKEANAYDfIMKLPhqfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 556 ATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQ 608
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
146-361 |
5.96e-29 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 117.97 E-value: 5.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 146 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIG 225
Cdd:cd18575 71 LRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 226 LSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLV 305
Cdd:cd18575 151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLV 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 306 YASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLGTfSIGHLAPNIEAFANARGAA 361
Cdd:cd18575 231 FGAIVFVLWLGAHDVLAGRMSAGELSQfVFYAVLAAG-SVGALSEVWGDLQRAAGAA 286
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1050-1261 |
6.04e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.82 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1205 DTESEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK11432 168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1046-1249 |
6.24e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.06 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqwlrahlgivsqepilfdcsi 1125
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP--------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 aeniaygdnsravsheeivRAAKEANIhQFIdslpdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL- 1204
Cdd:cd03216 70 -------------------RDARRAGI-AMV---------------YQLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 126927 1205 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1051-1232 |
7.03e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 117.19 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFDC 1123
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYGD--NSRAVSHEEIV-RAAKEAnihqfidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 126927 1201 TSALDTESEKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
391-618 |
7.89e-29 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 116.72 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEG-VVSIDGQDIRTINVRYLREII 469
Cdd:COG1119 4 LELRNVTV---RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVS---------QEPVL-------FATTiaeniryGR-EDVTMDEIEKAVKeanaydfIMKLPHqFDTLVGERGAQLSG 532
Cdd:COG1119 81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARE-------LLELLG-LAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGFD------GGV 604
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIThvlllkDGR 220
|
250
....*....|....
gi 126927 605 IVEQGNHDELMREK 618
Cdd:COG1119 221 VVAAGPKEEVLTSE 234
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
712-968 |
1.04e-28 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 117.62 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 712 GVLCAVINGCIQPVFAIVFSRIVGVFS-RDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMV 790
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASkESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 791 FKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGG 870
Cdd:cd18573 81 FKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 871 IIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFS 950
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250
....*....|....*...
gi 126927 951 YAACFRFGAYLVAQQLMT 968
Cdd:cd18573 239 LLSVLYYGGSLVASGELT 256
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
407-607 |
1.37e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.32 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLREIIGVVSQEP---VLFA 480
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIAENIRYG-REDVTMDEIEKAVKEANAYDfIMKLPhqfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10419 106 KTVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 560 LDTESEAVVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFDGGVIVE 607
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
391-584 |
1.96e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 114.84 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REIIGVVSQEPVLFAT-TIAENI-----RYGREDVTmdeiEKAVKEANAYDfimklphqfdtlVGERG----AQLSGGQK 535
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLdhypAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVI 584
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVL 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1046-1253 |
1.98e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 114.27 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKqlNVQWLRAHLGIVSQEPILF-DCS 1124
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYpHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:cd03301 89 VYDNIAFGLKLRKVPKDEIDErvreVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1201 TSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHG 1253
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
391-617 |
2.36e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQ---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-NVRYLR 466
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 EIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRI 538
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPHL-----------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 126927 617 E 617
Cdd:PRK13633 234 E 234
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
724-968 |
2.50e-28 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 116.58 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 724 PVFaivFSRIVGVFSRD--DDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISW 801
Cdd:cd18780 16 PYF---FGQVIDAVTNHsgSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 802 FDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQA 881
Cdd:cd18780 93 FD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 882 LKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYL 961
Cdd:cd18780 171 KKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRL 250
|
....*..
gi 126927 962 VAQQLMT 968
Cdd:cd18780 251 VIDGELT 257
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1049-1259 |
3.63e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK--QLNVQWLRAHLGIVSQEPILFDCSIA 1126
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 -ENIAYGDNSravsheeiVRAAKEANIHQFIDSLPDKYN--TRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK09493 95 lENVMFGPLR--------VRGASKEEAEKQARELLAKVGlaERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1204 LDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK09493 167 LDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
390-616 |
3.71e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 390 NLEFKNVHFNYpsrsEVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLREIi 469
Cdd:COG3840 1 MLRLDDLTYRY----GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFA-TTIAENI--------RYGREDVTmdEIEKAVKEANAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAI 540
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIglglrpglKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 541 ARALVRNPKILLLDEATSALD----TESEAVVQaalDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVD---ELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
..
gi 126927 615 MR 616
Cdd:COG3840 218 LD 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1051-1241 |
4.84e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.49 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEI---KQLNVQwLRAHLGIVSQEPILFD 1122
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQfiDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 126927 1203 ALDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1241
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1033-1254 |
5.39e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 115.28 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS---VFLDGKEIKQLNVQWLRA 1109
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIA 1183
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
143-339 |
9.79e-28 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 114.44 E-value: 9.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 143 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSP 222
Cdd:cd18552 71 VRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 223 LIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAY 302
Cdd:cd18552 151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 126927 303 LLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILL 339
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGEFISFITALLL 267
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
405-617 |
1.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYLREIIGVVSQEP--VLFA 480
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLPhqFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:PRK13637 99 ETIEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 559 ALD--TESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK13637 174 GLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1047-1260 |
1.15e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 112.77 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAHLGI--VSQEPILF-DC 1123
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENI---AYGDNSRAVSHEEIVRAA------KEanihqfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:COG0410 94 TVEENLllgAYARRDRAEVRADLERVYelfprlKE----------------RRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1195 LLLDEATSALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG0410 158 LLLDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
391-563 |
1.16e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 112.82 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIG 470
Cdd:cd03296 3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFA-TTIAENIRYG------REDVTMDEIEKAVKEanaydfIMKLPhQFDTLVGERGAQLSGGQKQRIAIARA 543
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEIRAKVHE------LLKLV-QLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180
....*....|....*....|
gi 126927 544 LVRNPKILLLDEATSALDTE 563
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAK 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
391-610 |
1.45e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 111.10 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHF---NYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLM-----QRLYDPLEGVVSIDGQDIRTINV 462
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKST---LLnalagRRTGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 463 RYlreIIGVVSQEPVLFAT-TIAENIrygredvtmdeiekavkeanayDFIMKLphqfdtlvgeRGaqLSGGQKQRIAIA 541
Cdd:cd03213 81 RK---IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 542 RALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGN 610
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
409-609 |
1.52e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 111.62 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVK---SGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ---DIR-TINVRYLREIIGVVSQEPVLFA- 480
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIAENIRYGREDVTMDEIEKAVKEANAYdfimklpHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDELLDL-------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 126927 561 DTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 609
Cdd:cd03297 163 DRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1033-1260 |
2.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.16 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-VQWLRAHL 1111
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqFIDSLPDKYNTRvgdKGTQLSGGQKQRIAIARALV 1189
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1190 RQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
391-634 |
2.10e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LEGVVSIDGQDIRTINVRYLRE 467
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEANA----YDFIMKLPhqfdtlvgergAQLSGGQKQRIA 539
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDElmre 617
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE---- 229
|
250
....*....|....*..
gi 126927 618 kgIYFKLVMTQTRGNEI 634
Cdd:PRK13640 230 --IFSKVEMLKEIGLDI 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1049-1247 |
2.60e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.76 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFL-DGKEIkqlnvqwlrahLgIVSQEPILFDCSIAE 1127
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLpdkynTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 126927 1208 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENG 1247
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1049-1262 |
2.76e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 112.59 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA---HLGIVSQEpilfdcsi 1125
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQD-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 aeniAYGDNSRAVSHEEIVR-----------AAKEANIHQFID--SLPDKYNTRVgdkGTQLSGGQKQRIAIARALVRQP 1192
Cdd:TIGR02769 97 ----SPSAVNPRMTVRQIIGeplrhltsldeSEQKARIAELLDmvGLRSEDADKL---PRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
391-606 |
2.90e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.06 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPK 549
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 550 ILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV 606
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
391-633 |
2.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.54 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 542
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQG------NHDEL 614
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGtpteifDHAEE 235
|
250 260
....*....|....*....|.
gi 126927 615 MREKG--IYFKLVMTQTRGNE 633
Cdd:PRK13648 236 LTRIGldLPFPIKINQMLGHQ 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
384-618 |
3.22e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 384 PDSImgnLEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ--DIRTIN 461
Cdd:PRK13636 2 EDYI---LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 VRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTM--DEIEKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQKQR 537
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 538 IAIARALVRNPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFDGGVIVEQGNHDE 613
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
....*
gi 126927 614 LMREK 618
Cdd:PRK13636 229 VFAEK 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
845-1265 |
3.48e-27 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 120.44 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 845 VILSLVYGWQ-----LTLLLVVIIPLIVLGGIIEMKLLSGQaLKDKKQLEISGKIATEAIENFRTIV----SLTREQKFE 915
Cdd:TIGR00957 445 VILALYFLWLnlgpsVLAGVAVMVLMVPLNAVMAMKTKTYQ-VAHMKSKDNRIKLMNEILNGIKVLKlyawELAFLDKVE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 916 TMYAQSLQVpyrnaMKKAHVFGITFSFTQAMMYFSYAACfRFGAYLVAQQlmtfENVMLVFSAVVfgAMAAGNTSSFA-- 993
Cdd:TIGR00957 524 GIRQEELKV-----LKKSAYLHAVGTFTWVCTPFLVALI-TFAVYVTVDE----NNILDAEKAFV--SLALFNILRFPln 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 994 --PDYAKAKVSAS---HIIRIIEKTPEIDSYSTEGLKPTLLEGN-VKFNGVQFNYpTRPNIPVLQGLSLEVKKGQTLALV 1067
Cdd:TIGR00957 592 ilPMVISSIVQASvslKRLRIFLSHEELEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVV 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1068 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAA 1147
Cdd:TIGR00957 671 GQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEAC 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1148 KeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL---DKAREGRT 1224
Cdd:TIGR00957 738 A---LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKT 814
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 126927 1225 CIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR00957 815 RILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
391-614 |
3.89e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFAT-TIAENIRYGREDVT---MD--EIEKAVKEANAYdfiMKLPHQFDTLVGErgaqLSGGQKQRIAIARA 543
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRgglIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 544 LVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1129 155 LSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1046-1247 |
4.06e-27 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 110.50 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH----LGIVSQEPILF 1121
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 DCSIAENIAYGDNSRAVSHEEIVRAAkeaNIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 1202 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENG 1247
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1050-1251 |
4.06e-27 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 110.99 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIKQLN----VQWLRAHLGIVSQE----P 1118
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILfdcSIAEN------IAYGDNSRAVSHEEIVRAAKEANIHQFidslPdkyntrvgdkgTQLSGGQKQRIAIARALVRQP 1192
Cdd:COG4181 104 TL---TALENvmlpleLAGRRDARARARALLERVGLGHRLDHY----P-----------AQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1193 HILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1051-1254 |
4.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.45 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEP--ILFDCSIA 1126
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYGDNSRAVSHEEIVRAAKEAnihqfIDSLPDKYNTrVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1206 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1038-1262 |
4.91e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 4.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1038 VQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL--RAHLGIVS 1115
Cdd:PRK13639 7 LKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1116 QEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqfidslpdkyNTRVGDKGTQ------LSGGQKQRIAIARA 1187
Cdd:PRK13639 85 QNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1188 LVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1033-1253 |
5.21e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 110.28 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILF-DCSIAENIAYGDNSR----AVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:cd03298 74 MLFQENNLFaHLTVEQNVGLGLSPGlkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1050-1265 |
5.73e-27 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 111.87 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI 1129
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 aygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1209
Cdd:cd03289 98 ---DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1210 KVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1040-1260 |
6.14e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.11 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP- 1118
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 -ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHqfIDSLpdKYNTRvgdKGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:PRK13642 92 nQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLA--VNML--DFKTR---EPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1198 DEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK13642 165 DESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
388-609 |
1.00e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDIRTINV 462
Cdd:PRK14247 1 MNKIEIRDLKVSF---GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 463 RYLREIIGVVSQEPVLFAT-TIAENIRYG----REDVTMDEIEKAVKEANAYdfiMKLPHQFDTLVGERGAQLSGGQKQR 537
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 609
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
391-618 |
1.06e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.41 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI----RTINVRY 464
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDeIEKAvkEANAYDFIMKLPHQFDTLvGERGAQLSGGQKQRIAIAR 542
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
391-586 |
1.13e-26 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 109.52 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT-TIAENIRY-----GREDVTMDEiekavkEANAYDFIMKLPHQFDTLVGergaQLSGGQKQRIAIARAL 544
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 586
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
709-971 |
1.26e-26 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 111.48 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIqPVFAivfSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFvtyfFQGFTFGKAGEILTKRVRY 788
Cdd:cd18572 2 FVFLVVAALSELAI-PHYT---GAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSG----LRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 789 MVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18572 74 DLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 869 -----GGIieMKLLSGQAlkdKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFT 943
Cdd:cd18572 152 itkvyGRY--YRKLSKEI---QDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVN 226
|
250 260
....*....|....*....|....*...
gi 126927 944 QAMMYFSYAACFRFGAYLVAQQLMTFEN 971
Cdd:cd18572 227 TLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
391-616 |
1.30e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 109.69 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINV-RYLREII 469
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFAT-TIAENIR---YGREDVtmDEIEKAVKEAnaYDFimklphqFDTLvGER----GAQLSGGQKQRIAIA 541
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgaYARRDR--AEVRADLERV--YEL-------FPRL-KERrrqrAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 542 RALVRNPKILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAEL 223
|
..
gi 126927 615 MR 616
Cdd:COG0410 224 LA 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
405-615 |
1.39e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.44 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-------------NVRYLREIIGV 471
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQEPVLFA-TTIAENIRygREDVTMDEIEKAVKEANAYDFIMKLPHQfDTLVGERGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK10619 97 VFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 551 LLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-DGGVIVEQGNHDELM 615
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1050-1249 |
1.40e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 110.13 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAHLGIVS--QEPILF-DCSIA 1126
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYG--------------DNSRAVSHEEIVRAAKEANIHQFidSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 1192
Cdd:COG0411 98 ENVLVAaharlgrgllaallRLPRARREEREARERAEELLERV--GLADRADEPAGN----LSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1193 HILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG0411 172 KLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-609 |
1.52e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.94 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKN--VHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLMQRLYDPLEGVVSIDGQDIRTINVRY 464
Cdd:COG4172 7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 LREI----IGVVSQEPV-----LFatTI----AENIR----YGREDVT------MDE--IEKAVKEANAYdfimklPHQf 519
Cdd:COG4172 86 LRRIrgnrIAMIFQEPMtslnpLH--TIgkqiAEVLRlhrgLSGAAARaralelLERvgIPDPERRLDAY------PHQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 520 dtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN 593
Cdd:COG4172 157 ----------LSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQiLDllkdlQRELGMALLLITHDLGVVRR 222
|
250
....*....|....*..
gi 126927 594 -ADVIAGFDGGVIVEQG 609
Cdd:COG4172 223 fADRVAVMRQGEIVEQG 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1049-1259 |
1.90e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAE 1127
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGdnsrAVSHEEIVRAAKEanihqfidsLPDKYNTRVGDKG------TQLSGGQKQRIAIARALVR------QPHIL 1195
Cdd:PRK13548 96 VVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1196 LLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK13548 163 LLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1050-1260 |
2.17e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.45 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--------KQLNVQWLRAHLGIVSQEPILF 1121
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 DC-SIAENIAYGDN-SRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK11264 98 PHrTVLENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1200 ATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK11264 171 PTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
390-612 |
3.08e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.95 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 390 NLEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG------QDIRTINVR 463
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 YLREIIGVVSQE----PVLfatTIAENIrygredvtmdeIEKAVK-----EANAYDFIMKLPH--QFDTLVGERGAQLSG 532
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENL-----------IEAPCKvlglsKEQAREKAMKLLArlRLTDKADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGN 610
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
..
gi 126927 611 HD 612
Cdd:COG4161 225 AS 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1049-1254 |
3.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.83 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQ--EPILFD 1122
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYGDNSRAVSHEEIVRAAKEA-NIHQFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1202 SALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1049-1261 |
3.21e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 114.78 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA----HLGIVSQEPI- 1119
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 ----LFdcSIAENIA-----YGDNSRAVSHEEIVRAAKEANIHQfidslPDKyntRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:COG4172 104 slnpLH--TIGKQIAevlrlHRGLSGAAARARALELLERVGIPD-----PER---RLDAYPHQLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1191 QPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4172 174 EPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1260 |
3.61e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.11 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYptRPNIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNV 1104
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1105 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqfID--SLPDKYNTRvgdKGTQLSGGQKQ 1180
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQ 1256
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....
gi 126927 1257 QLLA 1260
Cdd:PRK13634 232 EIFA 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
391-561 |
3.67e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 111.35 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYlrei 468
Cdd:PRK11432 7 VVLKNITKRFGSNT---VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALV 545
Cdd:PRK11432 80 ICMVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALI 152
|
170
....*....|....*.
gi 126927 546 RNPKILLLDEATSALD 561
Cdd:PRK11432 153 LKPKVLLFDEPLSNLD 168
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1033-1235 |
4.66e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.97 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVFLDGK-EI-------KQLNV 1104
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFfnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1105 QWLRAHLGIVSQEPILFDCSIAENIAYGDN----SRAVSHEEIVRAAKEANihqfidSLPDKYNTRVGDKGTQLSGGQKQ 1180
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTI 1235
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
388-561 |
4.67e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.80 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYP-SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylR 466
Cdd:COG4525 1 MSMLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 eiiGVVSQEPVLFA-TTIAENIRYGredVTMDEIEKAVKEANAydfimklpHQFDTLVGERGA------QLSGGQKQRIA 539
Cdd:COG4525 79 ---GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARA--------EELLALVGLADFarrriwQLSGGMRQRVG 144
|
170 180
....*....|....*....|..
gi 126927 540 IARALVRNPKILLLDEATSALD 561
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALD 166
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1051-1247 |
4.72e-26 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 107.94 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLrahlgIVSQEPILFD-CSIAENI 1129
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 AYGDNS--RAVSHEEivraaKEANIHQFIDSLPdkyNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:TIGR01184 76 ALAVDRvlPDLSKSE-----RRAIVEEHIALVG---LTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 126927 1207 ESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENG 1247
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1033-1259 |
6.42e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 108.25 E-value: 6.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-SVFLDGKEIKQLNVQWLRAHL 1111
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVS---QEPILFDCSIAENIAYGDNS-----RAVSHEEIVRAakEANIHQF-IDSLPDK-YNTrvgdkgtqLSGGQKQR 1181
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyREPTDEQRERA--RELLELLgLAHLADRpFGT--------LSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1182 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVIENGKVKEHGTH 1255
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGPK 227
|
....
gi 126927 1256 QQLL 1259
Cdd:COG1119 228 EEVL 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
409-616 |
6.96e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 107.52 E-value: 6.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylrEI----IGVVSQEPVLFAT-TI 483
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIarlgIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AENIRYG-----REDVTMDEIEKAVKEANAYDF----IMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:cd03219 93 LENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 555 EATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
403-609 |
7.18e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 107.36 E-value: 7.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQL-MQRLYDP--LEGVVSIDGQDIRtinvRYL-REIIGVVSQEPVL 478
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAiSGRVEGGgtTSGQILFNGQPRK----PDQfQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 479 FAT-TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHqfDTLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 557 TSALDTESE-AVVQAALDKAREGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03234 171 TSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
391-609 |
7.89e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.51 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTvALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRtINVRYLREIIG 470
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT-TIAENIRY-----GREDVTMD-EIEKAVKEANAYDFimklphqfdtlVGERGAQLSGGQKQRIAIARA 543
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1047-1261 |
7.96e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 7.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW-LRAHLGIVSQEPilfDCSI 1125
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNP---DNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 A-----ENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:PRK13633 99 VativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1197 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
409-601 |
1.16e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.95 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL-----EGVVSIDGQDI--RTINVRYLREIIGVVSQEPVLFAT 481
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 482 TIAENIRYGRE----DVTMDE-IEKAVKEANAYDFIMklphqfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PRK14243 106 SIYDNIAYGARingyKGDMDElVERSLRQAALWDEVK------DKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 126927 557 TSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFD 601
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1033-1262 |
1.23e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.38 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVqfNYPTRPNIPV----LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK----QLNV 1104
Cdd:PRK13641 3 IKFENV--DYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1105 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEivraAKEANIhqfidslpdKYNTRVG------DKGT-QLS 1175
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1176 GGQKQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHA 227
|
....*....
gi 126927 1254 THQQLLAQK 1262
Cdd:PRK13641 228 SPKEIFSDK 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
391-614 |
1.57e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.03 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKN--VHFNYPSRSEV-----QILK---GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI 460
Cdd:PRK15079 9 LEVADlkVHFDIKDGKQWfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 461 NVRYLREI---IGVVSQEPV-------LFATTIAENIRYGREDVTMDEIEKAVKEANAY-----DFIMKLPHQFdtlvge 525
Cdd:PRK15079 89 KDDEWRAVrsdIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 526 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDG 602
Cdd:PRK15079 163 -----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYL 237
|
250
....*....|..
gi 126927 603 GVIVEQGNHDEL 614
Cdd:PRK15079 238 GHAVELGTYDEV 249
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1050-1261 |
1.68e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 107.36 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-------QLNV------QWLRAHLGIVSQ 1116
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1117 EPILFD-CSIAENIAYGDN-----SRAVSHEEIVRAAKEANIHqfiDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVR 1190
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIqvlglSKQEARERAVKYLAKVGID---ERAQGKYPV-------HLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1191 QPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
141-361 |
2.09e-25 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 107.90 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 141 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAV 220
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 221 SPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAA 361
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1050-1253 |
2.27e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 105.35 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFD-CSIAEN 1128
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAY-----GDNSRAVsHEEIVRAAKEANihqfidsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:cd03264 93 LDYiawlkGIPSKEV-KARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1204 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1051-1261 |
2.87e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 109.03 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGkEIKQ--LNVQWLRAH---LGIVSQE 1117
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGG-EVLQdsARGIFLPPHrrrIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1118 PILFD-CSIAENIAYG-----DNSRAVSHEEIVRAAkeaNIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:COG4148 86 ARLFPhLSVRGNLLYGrkrapRAERRISFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1192 PHILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4148 152 PRLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1054-1262 |
3.15e-25 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 108.66 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYG-----DNSRAVSHEEIVRAAkeaNIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1204 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1033-1253 |
3.24e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 104.61 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlrAHLG 1112
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLKD-----------SAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1192 PHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
120-336 |
3.58e-25 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 107.13 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 120 IGAGVL--IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSIT 197
Cdd:cd18542 46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 198 TFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWA-KVLTSFTNKElQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERY 276
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFkKVRPAFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 277 NKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFS 336
Cdd:cd18542 205 DKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
712-997 |
3.84e-25 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 106.80 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 712 GVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHEtkrqNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVF 791
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTA----SLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 792 KSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGI 871
Cdd:cd18576 77 RHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 872 I---EMKLLSGQALkdkKQLEISGKIATEAIENFRTIVSLTREQkFETM-YAQSLQVPYRNAMKKAHVFGITFSFTQAMM 947
Cdd:cd18576 155 LfgrRIRKLSKKVQ---DELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 126927 948 YFSYAACFRFGAYLVAQQLMTFENvmlVFSAVVFGAMAAGNTSSFAPDYA 997
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGD---LVAFLLYTLFIAGSIGSLADLYG 277
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1047-1253 |
4.65e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP-IL 1120
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1121 FDCSIAENIAYG------DNSRAVSHEEIVRAAKEAnihQFIDSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1194
Cdd:PRK14247 95 PNLSIFENVALGlklnrlVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1195 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIENGKVKEHG 1253
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1049-1262 |
4.69e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAE 1127
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGdNSRAVSH--------EEIVRAAKEANihqFIDSLPDKyntRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK11231 96 LVAYG-RSPWLSLwgrlsaedNARVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1200 ATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK11231 165 PTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
120-335 |
4.75e-25 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 106.63 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 120 IGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTF 199
Cdd:cd18784 45 LAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 200 LAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKN 279
Cdd:cd18784 125 IGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEK 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 280 LEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSiGEVLTVFF 335
Cdd:cd18784 205 LKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQIS-GGNLISFI 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
406-614 |
4.82e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 107.74 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLREIIGVVSQ-------- 474
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQnpygslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 475 ---------EPVLFATTIAENIRygREDVtMDEIEKAVKEANAYDfimKLPHQFdtlvgergaqlSGGQKQRIAIARALV 545
Cdd:PRK11308 108 rkkvgqileEPLLINTSLSAAER--REKA-LAMMAKVGLRPEHYD---RYPHMF-----------SGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 546 RNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIV-IAHRLSTVRNA--DVIAGFDGGViVEQGNHDEL 614
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEHIadEVMVMYLGRC-VEKGTKEQI 242
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
388-614 |
5.07e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 108.58 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVhfnYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdiRTINVRYLRE 467
Cdd:PRK11000 1 MASVTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEPVLFA-TTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARAL 544
Cdd:PRK11000 76 GVGMVFQSYALYPhLSVAENMSFGLKlaGAKKEEINQRVNQVAE---VLQLAH----LLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 545 VRNPKILLLDEATSALDTESEavVQ-----AALDKaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALR--VQmrieiSRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
391-612 |
6.37e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.10 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG------QDIRTINVRY 464
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 LREIIGVVSQEPVLFA-TTIAENIrygredvtmdeIEKAVK-----EANAYDFIMKLphqFDTLVGERGA-----QLSGG 533
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNL-----------IEAPCRvlglsKDQALARAEKL---LERLRLKPYAdrfplHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 534 QKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNH 611
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAqIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
.
gi 126927 612 D 612
Cdd:PRK11124 226 S 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1262 |
7.92e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAH 1110
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1111 LGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARAL 1188
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1189 VRQPHILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
388-609 |
8.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.60 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGnLEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI----N 461
Cdd:PRK13649 1 MG-INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 VRYLREIIGVVSQ--EPVLFATTIAENIRYGRED--VTMDEIEKAVKEANAYDFIMklphqfDTLVGERGAQLSGGQKQR 537
Cdd:PRK13649 80 IKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
391-617 |
8.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.45 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN-VRYLREII 469
Cdd:PRK13644 2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEP--VLFATTIAENIRYGREDVTMD--EIEKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQKQRIAIARALV 545
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 546 RNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
407-563 |
8.59e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLReiIGVVSQEPVLFA-TTIAE 485
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 486 NIRYG------REDVTMDEIEKAVkeanaydfiMKLPH--QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
....*.
gi 126927 558 SALDTE 563
Cdd:PRK10851 165 GALDAQ 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1049-1253 |
9.31e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.01 E-value: 9.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQlnvQWLRAHLGIVSQEPILFDC-SI 1125
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 AENIAYgdnsravsheeivrAAKeanihqfidsLpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:cd03213 100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1206 TESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHG 1253
Cdd:cd03213 144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1050-1253 |
1.09e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 103.51 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEW-LERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126927 1209 EKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03269 164 VELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
404-602 |
1.14e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 103.56 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 404 SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVV----SIDGQDIRTINVRYLREIIGVVSQEPVLF 479
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 480 ATTIAENIRYGREdvTMDEIEKAVKEANAYD-FIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:cd03290 92 NATVEENITFGSP--FNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 126927 559 ALDTE-SEAVVQAALDK--AREGRTTIVIAHRLSTVRNAD-VIAGFDG 602
Cdd:cd03290 170 ALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADwIIAMKDG 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
391-611 |
1.36e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 110.58 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REIIGVVSQEPVLFA-TTIAENIRYgreDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VIAGFDGGVIVEQGNH 611
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAErVIEIRDGEIVRNPPAQ 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1034-1230 |
1.45e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.56 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYP-TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAHLG 1112
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEanihqfidslpdkYNTRVGDKGT------QLSGGQKQRIAIA 1185
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126927 1186 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1230
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1050-1259 |
1.89e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILF-D 1122
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1203 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1051-1261 |
2.38e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.43 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQEPilfdcsiae 1127
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 niaYGD-NSRA----------VSHEEIVRAAKEANIHQFIdslpdkynTRVGDKGTQ-------LSGGQKQRIAIARALV 1189
Cdd:PRK11308 102 ---YGSlNPRKkvgqileeplLINTSLSAAERREKALAMM--------AKVGLRPEHydryphmFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1190 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1048-1267 |
3.64e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.07 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlnVQWLRAHLGIVSQEPILF-DCSIA 1126
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1203 ALDTESEKVVQ-EALD-KAREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS 1267
Cdd:PRK11607 179 ALDKKLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
391-609 |
3.97e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIR----TINVRY 464
Cdd:PRK13641 3 IKFENVDYIYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPhqfDTLVGERGAQLSGGQKQRIAIAR 542
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLS---EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 543 ALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHrlstvrNADVIAGFDGGVIV-EQG 609
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVlEHG 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
398-621 |
4.08e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.93 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 398 FNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSID----GQDIRTI------------N 461
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 VRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTMDEIEkAVKEANAYDFIMKLPHQFDtlvgERGA-QLSGGQKQRI 538
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYL----ERSPfGLSGGQKRRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 539 AIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFT 265
|
....*
gi 126927 617 EKGIY 621
Cdd:PRK13631 266 DQHII 270
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
389-587 |
4.32e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 GNLEFKNVHFNYPSRSEvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSI-DGQDIrtinvryLre 467
Cdd:COG4178 361 GALALEDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 iigVVSQEPVLFATTIAENIRY--GREDVTMDEIEKAVKEANaydfimkLPH---QFDTlVGERGAQLSGGQKQRIAIAR 542
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGHlaeRLDE-EADWDQVLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR 587
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
391-561 |
4.36e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIRYGRedvtmdEIEKAVKEANAY-DFIMK--LPhqfDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 126927 548 PKILLLDEATSALD 561
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
388-561 |
4.36e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 105.31 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYPSRseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRyLRE 467
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IiGVVSQEPVLFA-TTIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLphqfDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:PRK11650 78 I-AMVFQNYALYPhMSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAI 149
|
170
....*....|....*..
gi 126927 545 VRNPKILLLDEATSALD 561
Cdd:PRK11650 150 VREPAVFLFDEPLSNLD 166
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
401-609 |
4.88e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 101.68 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 401 PSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPVLFA 480
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 -TTIAENIRY--GREDVTMDEIEKAVKEanaydFIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:cd03266 92 rLTARENLEYfaGLYGLKGDELTARLEE-----LADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 558 SALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQG 609
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1265 |
4.97e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.55 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ----LL---------ERFY-----DPMAGSVFLDGKEIKq 1101
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIkskygtiqvGDIYigdkkNNHELITNPYSKKIK- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1102 lNVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEivrAAKEANIHQFIDSLPDKYNTRvgdKGTQLSGGQK 1179
Cdd:PRK13631 110 -NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSYLER---SPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1180 QRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQ 1257
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYE 262
|
....*...
gi 126927 1258 LLAQKGIY 1265
Cdd:PRK13631 263 IFTDQHII 270
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
412-609 |
7.01e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.03 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG 490
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 491 R------EDVTMDEIEKAVKEANAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:cd03298 95 LspglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 126927 565 EAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
389-625 |
7.80e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.48 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 GNLEFKNVHFNYpsRSEVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEPVLFATTIAENIRYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALV-R 546
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 547 NPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL-MREKGIYFKLV 625
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1043-1253 |
9.65e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.91 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFD 1122
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 -CSIAENIAY-GDnsravsheeiVRAAKEANIHQFIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHI 1194
Cdd:cd03266 92 rLTARENLEYfAG----------LYGLKGDELTARLEELADRLgmeellDRRVGG----FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1195 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1055-1262 |
9.95e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 9.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikQLNVQWLRAHLGIVSQEPILFD-CSIAENIAYGD 1133
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1134 NS----RAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1205
Cdd:PRK10771 97 NPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1206 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1033-1254 |
1.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVqfNYPTRPNIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNV 1104
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1105 QWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKE-----ANIHQFIDSLPdkyntrvgdkgTQLSGG 1177
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
405-609 |
1.11e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 100.37 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI-RTINVRylrEIIGVVSQEPVLFAT-T 482
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEAL---RRIGALIEAPGFYPNlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 483 IAENIR-----YGREDVTMDEIEKAVKEANAYDfimklphqfdtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:cd03268 89 ARENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 558 SALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03268 155 NGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
391-618 |
1.40e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 100.68 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI-RTINVRYLREII 469
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFAT-TIAENIRYGREdvTMDEIEKAVKeanayDFIMKL-PHQFDTLvGERGAQLSGGQKQRIAIARALVRN 547
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
706-1262 |
1.42e-23 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 108.84 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 706 WPYLLVGVLCAV--INGCIQPvfaIVFSRIVGVFsrDDDHETKRQNCnlfslFFLVMGL-ISFV--TYFFQGFTFGKAGE 780
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASY--DPFNAPEREIA-----YYLALGLcLLFIvrTLLLHPAIFGLHHL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 781 ILTKRVRY--MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMG-ARLAVVTQNVANLGTGVILSLVYGWQLTL 857
Cdd:TIGR01271 150 GMQMRIALfsLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLAlAHFVWIAPLQVILLMGLIWELLEVNGFCG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 858 LLVVIIPLIVLGGIIEMKLlsgqALKDKKQLEISGKIA--TEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHV 935
Cdd:TIGR01271 228 LGFLILLALFQACLGQKMM----PYRDKRAGKISERLAitSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 936 fgitfsftqamMYFSYAACFrFGAYLVaqqlmtfenvmlVFSAVVFGAMAAG-------NTSSFA-----------PDYA 997
Cdd:TIGR01271 304 -----------RYFYSSAFF-FSGFFV------------VFLSVVPYALIKGiilrrifTTISYCivlrmtvtrqfPGAI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 998 KAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLE---GNVK----------FNGVQFNYPTR--PN--------------I 1048
Cdd:TIGR01271 360 QTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEvemVNVTaswdegigelFEKIKQNNKARkqPNgddglffsnfslyvT 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAEN 1128
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRAVSHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1209 EKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
100-361 |
1.47e-23 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 102.49 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 100 IISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWcLAAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDV 178
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLI-FGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 179 SKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLA 258
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 259 AIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSIL 338
Cdd:cd18541 188 GIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVA--FNSY 265
|
250 260
....*....|....*....|....*...
gi 126927 339 LG-----TFSIGHLAPNIEafanaRGAA 361
Cdd:cd18541 266 LGmliwpMMALGWVINLIQ-----RGAA 288
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
391-609 |
1.73e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.07 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDIRTINVR-- 463
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 YLREIIGVVSQEPVLFA-TTIAENIRYG-------REDVTMDE-IEKAVKEANAYDfimklphQFDTLVGERGAQLSGGQ 534
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 535 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFDGGVIVEQG 609
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
408-618 |
2.49e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVL-FATTIAEN 486
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 487 IRYGR------------EDVTMdeIEKAVKEAnaydfimklphQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:PRK11231 97 VAYGRspwlslwgrlsaEDNAR--VNQAMEQT-----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 555 EATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1050-1258 |
2.51e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.24 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGdNSRAVSHEEIVRAAKEANIHQFID-----SLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK10851 95 IAFG-LTVLPRRERPNAAAIKAKVTQLLEmvqlaHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1204 LDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1050-1256 |
2.59e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP------MAGSVFLDGKEIKQLNVQWLRAHLGIVSQE----PI 1119
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPrsgtlnIAGNHFDFSKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 LfdcSIAEN-IAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:PRK11124 97 L---TVQQNlIEAPCRVLGLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1195 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQ 1256
Cdd:PRK11124 163 LLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
423-564 |
2.94e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 102.87 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 423 ALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG---QDIRT-INV-RYLREIiGVVSQEPVLFAT-TIAENIRYGRedvtm 496
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLpPHRRRI-GYVFQEARLFPHlSVRGNLLYGR----- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 497 deieKAVKEANAYDfimklphQFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:COG4148 103 ----KRAPRAERRI-------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
391-618 |
3.17e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.25 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI----RTINVRY 464
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQ------FDtlvgergaqLSGGQKQ 536
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEEllarspFE---------LSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 537 RIAIARALVRNPKILLLDEATSALDTESEAVVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHD 612
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*.
gi 126927 613 ELMREK 618
Cdd:PRK13634 232 EIFADP 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1050-1254 |
3.25e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 99.52 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAHLGI--VSQEPILF-DCSIA 1126
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYGDNSRAVSHEEIVraakeANIHQFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIP-----DEIYELFPVLKEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1207 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1254
Cdd:TIGR03410 165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
412-618 |
3.34e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 102.88 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG---QDIRT-INVRYLREIIGVVSQEPVLFA-TTIAEN 486
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 487 IRYGREDVTMDEieKAVKEANAYDfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 566
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIE-LLGIGH----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 567 VVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:TIGR02142 169 EILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1044-1251 |
3.52e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.53 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN----------VQWL------ 1107
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1108 ----RAHLGIVSQEPI--LFDCSIAEniaygdnsRAVSHEEIVRAAKEANIHqfIDSLPdkyntrvgdkgTQLSGGQKQR 1181
Cdd:PRK10419 101 avnpRKTVREIIREPLrhLLSLDKAE--------RLARASEMLRAVDLDDSV--LDKRP-----------PQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1182 IAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKE 1251
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1048-1247 |
3.79e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 99.43 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikqlnvQW-------------LRAH-LGI 1113
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG------GWvdlaqaspreilaLRRRtIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQ---------------EPILfdcsiaeniaygdnSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyNTrvgdkgtqL 1174
Cdd:COG4778 98 VSQflrviprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP--AT--------F 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1175 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENG 1247
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
391-588 |
3.91e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.55 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVH--FNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLR-E 467
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEPVL---FATTIAEN------------IRYGREDVTMDEIEKAVKEANaydfiMKLPHQFDTLVGergaQLSG 532
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDTKVG----LLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRL 588
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1032-1255 |
4.02e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 4.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1032 NVKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG------KEIKQLNVQ 1105
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1106 WLRAHLGIVSQE----PILfdcSIAENIAYG-----DNSRAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSG 1176
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1177 GQKQRIAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
.
gi 126927 1255 H 1255
Cdd:COG4161 225 A 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1046-1230 |
4.20e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAHLGIVSQ-EPILFDCS 1124
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQnEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAYGDNSRAVSheeivRAAKEANIHQFIdslpdkynTRVGDKGT------QLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:PRK11248 87 VQDNVAFGLQLAGVE-----KMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....
gi 126927 1199 EATSALDTESEKVVQEALDK--AREGRTCIVIAH 1230
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
409-615 |
4.76e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.19 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTI 483
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AENIRYGREdvtMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK10070 124 LDNTAFGME---LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 564 SEAVVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
393-618 |
4.84e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 393 FKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGqdirtiNVRylreiIGVV 472
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 473 SQEPVLFAT-TIAENIRYGREDVT-----MDEIEKAVK-----------------EANAYDF-------IMKL---PHQF 519
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELRaleaeLEELEAKLAepdedlerlaelqeefeALGGWEAearaeeiLSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 520 DTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqaaldKAREGrTTIVIAH-R--LSTVr 592
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV- 215
|
250 260
....*....|....*....|....*..
gi 126927 593 nADVIAGFDGGVIVE-QGNHDELMREK 618
Cdd:COG0488 216 -ATRILELDRGKLTLyPGNYSAYLEQR 241
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1032-1205 |
6.08e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.23 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1032 NVKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGSVFLDGKEIKQLnvqwlr 1108
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1109 ahlgivsqEPILFDC-------------SIAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkg 1171
Cdd:PRK11650 72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKP----------- 132
|
170 180 190
....*....|....*....|....*....|....
gi 126927 1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK11650 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1049-1254 |
6.25e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 6.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGSVFLDGKEIKQLNVQwLRAHLGI-VS-QEPI---- 1119
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 ------LfdcSIAENIAYGDNSRAV-SHEEIVRAAKEANihqfidsLPDKYNTR---VGdkgtqLSGGQKQRIAIARALV 1189
Cdd:COG0396 92 vsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1190 RQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
405-586 |
6.48e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 98.66 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ----DI-----RTI-NVRylREIIGVVSQ 474
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaqaspREIlALR--RRTIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 475 epvlFATTIAeniRYGREDVTMDE-IEKAVKEANAYDFIMKLPHQFDtlVGERGAQL-----SGGQKQRIAIARALVRNP 548
Cdd:COG4778 101 ----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIADP 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 126927 549 KILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAH 586
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
409-614 |
8.73e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.21 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPvlfattIAENIR 488
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 489 YGREDVTM---------DEIEKAVKEANAYdfiMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 560 LDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1051-1249 |
8.73e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.95 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-VQWLRAHLGIVSQEPILFDC-SIAEN 1128
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRAVSHEEIVRAAKEanihqfIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 126927 1203 AL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:COG3845 171 VLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-614 |
1.06e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.97 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ------DIRTINVRYLREIIGVVSQEPVLFA- 480
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIAENIRYGREDVTMD---EIEKAVKEANAYDFIMKLPHqfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKekrEIKKIVEECLRKVGLWKEVY--DRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 558 SALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1050-1253 |
1.18e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.76 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEIKQLNVQWL--RAHLGIVSQEPILF- 1121
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 DCSIAENIAYGD--NSRAVSHEEI---VR-AAKEAnihqfidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKKELderVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1196 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIENGKVKEHG 1253
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
409-586 |
1.19e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 97.92 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLreiigVVSQEPVLFA-TTIAENI 487
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYG----REDVTMDEIEKAVKEANAydfIMKLPHQFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEEHIA---LVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*
gi 126927 564 SEAVVQAALDKARE--GRTTIVIAH 586
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1049-1262 |
1.56e-22 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 99.16 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAEN 1128
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRAVSHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1209 EKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1050-1249 |
1.58e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 97.73 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVFLDGKEIKQlnVQWLRaHLGIVSQEPILFDC-SI 1125
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 AENIAYGDNSRavSHEEIVRAAKEANIHQFidSLPDKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03234 99 RETLTYTAILR--LPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 126927 1205 DTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIENGKV 1249
Cdd:cd03234 175 DSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
388-614 |
1.64e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYpsRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:PRK13652 1 MHLIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEP--VLFATTIAENIRYGREDVTMDE------IEKAVKEANAYDFIMKLPHqfdtlvgergaQLSGGQKQRIA 539
Cdd:PRK13652 79 FVGLVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1040-1232 |
2.12e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRA-HLGIVSQEP 1118
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAkYIGRVFQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILFDC---SIAENIAYGDN---SRAVSheeivRAAKEANIHQFIDS-------LPDKYNTRVGdkgtQLSGGQKQRIAIA 1185
Cdd:COG1101 90 MMGTApsmTIEENLALAYRrgkRRGLR-----RGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 1186 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRL 1232
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1055-1259 |
2.13e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL----RAHLGIVSQE-PILFDCSIAENI 1129
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 AYGDNSRAVSHEE----IVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK10070 128 AFGMELAGINAEErrekALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1206 TESEKVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
86-588 |
2.39e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 104.61 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 86 LPSITNQSGPNST----------LIISNSSleeemAIYAYY-YTGIGAGVLIVAYIQ---VSLWCLAAGRQIHKirqKFF 151
Cdd:TIGR01271 894 NPSAPNYVDQQHAnasspdvqkpVIITPTS-----AYYIFYiYVGTADSVLALGFFRglpLVHTLLTVSKRLHE---QML 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 152 HAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFL-AGFIIGFISGWkltlVILAVSPLIGLSSAL 230
Cdd:TIGR01271 966 HSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLgAIFVVSVLQPY----IFIAAIPVAVIFIML 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 231 WAKVL-TSFTNKELQAYAKAGAVAEEV--LAAIRTVIAFGGQQkelerYNKNLeeaknvgIKKAITASISIGIAYL---- 303
Cdd:TIGR01271 1042 RAYFLrTSQQLKQLESEARSPIFSHLItsLKGLWTIRAFGRQS-----YFETL-------FHKALNLHTANWFLYLstlr 1109
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 304 -------LVYASYALAFWY---GTSLVlsNEYSIGEVLTVFFSILlGTFSIGhLAPNIEAFANARGAAfEIFKIID--NE 371
Cdd:TIGR01271 1110 wfqmridIIFVFFFIAVTFiaiGTNQD--GEGEVGIILTLAMNIL-STLQWA-VNSSIDVDGLMRSVS-RVFKFIDlpQE 1184
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 372 PSIDSFSTKGYKPDSIM--------------GNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ 437
Cdd:TIGR01271 1185 EPRPSGGGGKYQLSTVLvienphaqkcwpsgGQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 438 LMQRLYDPlEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI----RYGREdvtmdEIEKAVKEANAYDFIM 513
Cdd:TIGR01271 1264 ALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdpyeQWSDE-----EIWKVAEEVGLKSVIE 1337
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 514 KLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:TIGR01271 1338 QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
402-563 |
2.78e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LEGVVSIDGQDIRTINVrYLREIiGVVSQEPVL 478
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA-EQRRI-GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 479 FA-TTIAENIRYG-REDVTM----DEIEKAVKEANaydfimkLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:COG4136 88 FPhLSVGENLAFAlPPTIGRaqrrARVEQALEEAG-------LAGFADRDP----ATLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 126927 553 LDEATSALDTE 563
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
995-1275 |
3.11e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.48 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 995 DYAKAKVSASHIIRiiektPEIDSYSTEGLKPTLLEGNVKFNGVQFnYPTRPNIpVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:PTZ00243 627 DYGSPSSASRHIVE-----GGTGGGHEATPTSERSAKTPKMKTDDF-FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGK 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1075 STVVQLLERFYDPMAGSVfldgkeikqlnvqWLRAHLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAAK-EANIH 1153
Cdd:PTZ00243 700 STLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQlEADLA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1154 QfidsLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:PTZ00243 767 Q----LGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQV 842
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 126927 1233 STIQNADLIVVIENGKVKEHGTHQQlLAQKGIYFSMVQAGAKR 1275
Cdd:PTZ00243 843 HVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKEN 884
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
391-618 |
3.14e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.53 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVL-FATTIAENIRYGREDVT--MDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVR- 546
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRAPHGlsRAEDDALVAAALA---QVDLAH----LAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 547 -----NPKILLLDEATSALD-TESEAVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
392-621 |
3.68e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQEPVlFAT--TIAENIRYGR----------EDvtmdeiEKAVKEANAYDFIMKLPHQF-DtlvgergaQLSGGQKQRI 538
Cdd:COG4604 80 LRQENH-INSrlTVRELVAFGRfpyskgrltaED------REIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFDGGVIVEQGNH 611
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTP 220
|
250
....*....|...
gi 126927 612 DELMRE---KGIY 621
Cdd:COG4604 221 EEIITPevlSDIY 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1049-1260 |
3.88e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 96.46 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAHLGI--VSQEPILF-DCSI 1125
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 AENIAYGDNSRAVSHEEIVRAAkEANIHQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1205 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1261 |
3.92e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.95 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1042 YPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP--I 1119
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 LFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSAlhmlGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1196 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
391-609 |
4.17e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.09 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSR--------SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYdPLEGVVSIDGQDIRTINV 462
Cdd:PRK15134 276 LDVEQLQVAFPIRkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 463 RYL---REIIGVVSQEP---------VLfaTTIAENIRYGREDVTMDEIEKAVKEAnaydfiMKlphqfdtlvgERG--- 527
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME----------EVGldp 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 528 -------AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNA--DV 596
Cdd:PRK15134 417 etrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQV 496
|
250
....*....|...
gi 126927 597 IAGFDGGViVEQG 609
Cdd:PRK15134 497 IVLRQGEV-VEQG 508
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
400-595 |
5.23e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 400 YPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGqdirTINVRYLREIIGVVSQEPVlf 479
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 480 atTIAENI------------RYGREDvtmdeiEKAVKEAnaydfIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:NF040873 73 --TVRDLVamgrwarrglwrRLTRDD------RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 548 PKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRNAD 595
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
391-614 |
5.37e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.52 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQilkGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINvRYLREIiG 470
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPI-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKE----ANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIARA 543
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEmlglVHMQEFAKRKPHQ-----------LSGGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1049-1272 |
6.30e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.00 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEP--ILFDCS 1124
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAYGDNSRAVSHEEIVRAAKEANihqfidSLPDKYNTRvgDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEAL------TLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1204 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQKGIyfsMVQAG 1272
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA---MEQAG 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1049-1242 |
7.01e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYGDNSRavsHEEIVRAAKEANIHQFidSLPDKyntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:PRK10247 101 LIFPWQIR---NQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 126927 1208 SEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIV 1242
Cdd:PRK10247 172 NKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1011-1252 |
7.65e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1011 EKTPEIDSYSTEGLKPTLLEgnvkFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG 1090
Cdd:COG0488 298 DKTVEIRFPPPERLGKKVLE----LEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1091 SVFLdGKEIKqlnvqwlrahLGIVSQEPILFDC--SIAENIAygdnsravsheEIVRAAKEANIHQFIDSL---PDKYNT 1165
Cdd:COG0488 371 TVKL-GETVK----------IGYFDQHQEELDPdkTVLDELR-----------DGAPGGTEQEVRGYLGRFlfsGDDAFK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1166 RVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIV 1242
Cdd:COG0488 429 PVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRIL 500
|
250
....*....|
gi 126927 1243 VIENGKVKEH 1252
Cdd:COG0488 501 EFEDGGVREY 510
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
389-588 |
9.26e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 96.85 E-value: 9.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 389 GNLEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQEPVLFATTIAENIR-YGREdvTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-592 |
9.84e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL---YDPLEGVVSIDGQDIRtinvrylre 467
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKST---LMKILyglYQPDSGEILIDGKPVR--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 I----------IGVVSQEPVLFAT-TIAENIRYGREDVT-----MDEIEKAVKE-ANAYDFIMKLphqfDTLVGergaQL 530
Cdd:COG3845 71 IrsprdaialgIGMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 531 SGGQKQRIAIARALVRNPKILLLDEATSALdTESEAV-VQAALDK-AREGRTTIVIAHRLSTVR 592
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVL-TPQEADeLFEILRRlAAEGKSIIFITHKLREVM 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
391-617 |
9.99e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.90 E-value: 9.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQR-LYDPLEGVVSIDGQDI--RTINVR--- 463
Cdd:COG0396 1 LEIKNLHV---SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHpKYEVTSGSILLDGEDIleLSPDERara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 -------YLREIIGV-VSQepvlFATTIAENIRygREDVTMDEIEKAVKEANAydfIMKLPHQFdtlvGERG--AQLSGG 533
Cdd:COG0396 78 giflafqYPVEIPGVsVSN----FLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGN 610
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*..
gi 126927 611 HdELMRE 617
Cdd:COG0396 225 K-ELALE 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1042-1244 |
1.18e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1042 YPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlrahlgiVSQEPILF 1121
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 DCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqFIDSLpdkynTRVGDKG------TQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAA----VDDAL-----ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 126927 1196 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1244
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1044-1259 |
1.30e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.76 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FD 1122
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENIAYGDN---SRAVSHEEIVRAAKE-----ANIHQFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVEramerTGVAQFADR-----------PVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1195 LLLDEATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK09536 161 LLLDEPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1048-1251 |
1.89e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW---LRA-HLGIVSQEPILFDC 1123
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAkHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIA-ENIAY-----GDNSRAvSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:PRK10584 103 LNAlENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1198 DEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:PRK10584 171 DEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
100-336 |
2.07e-21 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 96.30 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 100 IISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVS 179
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 180 KINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAA 259
Cdd:cd18544 110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 260 IRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18544 190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG-VLYAFIQ 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1026-1248 |
4.29e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.46 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1026 PTLLE--GNVK-FNGVqfnyptrpniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GSVFLDGKEI 1099
Cdd:PRK13549 3 EYLLEmkNITKtFGGV----------KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1100 KQLNVQWL-RAHLGIVSQEPILF-DCSIAENIAYGD---NSRAVSHEEIVRAAKE--ANIHQFIDSlpdkyNTRVGDkgt 1172
Cdd:PRK13549 72 QASNIRDTeRAGIAIIHQELALVkELSVLENIFLGNeitPGGIMDYDAMYLRAQKllAQLKLDINP-----ATPVGN--- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1173 qLSGGQKQRIAIARALVRQPHILLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:PRK13549 144 -LGLGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
119-343 |
4.64e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 95.27 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 119 GIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITT 198
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 199 FLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNK 278
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 279 NLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFSILLGTFS 343
Cdd:cd18564 222 ENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYK 285
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1035-1262 |
4.69e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1035 FNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlnvqwlRAHLGIV 1114
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1115 SQEPILFD-CSIAENIAYGDNSR--------------AVSHEEIVRAAK-------------EANIHQFIDSL---PDKY 1163
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleaklAEPDEDLERLAElqeefealggweaEARAEEILSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1164 NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH-R--LSTIqnA 1238
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--A 216
|
250 260
....*....|....*....|....*
gi 126927 1239 DLIVVIENGKVKEH-GTHQQLLAQK 1262
Cdd:COG0488 217 TRILELDRGKLTLYpGNYSAYLEQR 241
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
145-334 |
5.37e-21 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 94.71 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 145 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSI--TTFLAGFIIGFisGWKLTLVILAVSP 222
Cdd:cd18590 70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLvkTLGMLGFMLSL--SWQLTLLTLIEMP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 223 LIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAY 302
Cdd:cd18590 148 LTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRR 227
|
170 180 190
....*....|....*....|....*....|..
gi 126927 303 LLVYASYALAFWYGTSLVLSNEYSIGEVLTVF 334
Cdd:cd18590 228 VLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1040-1272 |
5.38e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.44 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdgkeikqlnvqwLRAHLGIVSQEPI 1119
Cdd:PLN03232 622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 LFDCSIAENIAYGDNSRAvshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PLN03232 690 IFNATVRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1200 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQlLAQKGIYFS--MVQAG 1272
Cdd:PLN03232 767 PLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKklMENAG 841
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1049-1199 |
6.72e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.17 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGSVFLDGKEIKQLNVqWLRAHLGI--VSQEPIL 1120
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1121 F-DCSIAENIaygdnsRAVSheEIVRAAKEAnIHQFIDSLPDKYN-TRVGD-KGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:COG1137 90 FrKLTVEDNI------LAVL--ELRKLSKKE-REERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILL 160
|
..
gi 126927 1198 DE 1199
Cdd:COG1137 161 DE 162
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
407-615 |
9.96e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 92.61 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINV-RYLREIIGVVSQEPVLFAT-TIA 484
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 485 ENIRYGREDVTMDEIEKAVK-EANAYDF-IMKLPHQFdtlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKlEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 563 ESEAVVQAALDKAREGRTTIVIA-HR----LSTVRNADVIagFDGGVIVEqGNHDELM 615
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYII--YEGKVLAE-GTPEEIA 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1258 |
1.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.00 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV---FLDGKEIKQL-------------- 1102
Cdd:PRK13651 12 FNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTkekekvleklviqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1103 -------NVQWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEanihqFID--SLPDKYNTRvgdKG 1171
Cdd:PRK13651 92 trfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIElvGLDESYLQR---SP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIENGK- 1248
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKi 243
|
250
....*....|
gi 126927 1249 VKEHGTHQQL 1258
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1036-1249 |
1.47e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.82 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1036 NGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----MAGSVFL-DGKEIKQLNVQWLRa 1109
Cdd:PRK11247 16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 hlgivsqepILFDCSIAENIAYGdnsravsheeiVRAAKEANIHQFIDS--LPDkyntRVGDKGTQLSGGQKQRIAIARA 1187
Cdd:PRK11247 92 ---------LLPWKKVIDNVGLG-----------LKGQWRDAALQALAAvgLAD----RANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKV 1249
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
391-587 |
1.61e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 89.91 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDirtiNVRYLreiig 470
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 vvSQEPVLFATTIAENIRYGREDVtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03223 70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 126927 551 LLLDEATSALDTESEAvvqAALDKAREGRTTIV-IAHR 587
Cdd:cd03223 113 VFLDEATSALDEESED---RLYQLLKELGITVIsVGHR 147
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
406-616 |
1.63e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.41 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--------------RTI-NVRYLRE--- 467
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriarlgiaRTFqNPRLFPEltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 ----IIGVVSQEPVLFATTIAENIRYGREDvtmDEIEKAVKEANAydfIMKLPHQFDTLVGErgaqLSGGQKQRIAIARA 543
Cdd:COG0411 97 lenvLVAAHARLGRGLLAALLRLPRARREE---REARERAEELLE---RVGLADRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 544 LVRNPKILLLDEATSAL-DTESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1050-1260 |
1.64e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-----SVFLDGKEI-KQLNVQWLRAHLGIVSQEPILFDC 1123
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYGDNSRAVSHEEIVRAAKEANIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1204 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1026-1260 |
1.97e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1026 PTLLEgnvkFNGVQFNYPTRPNI--------PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVFLDGK 1097
Cdd:PRK15134 273 SPLLD----VEQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1098 EIKQLNVQWL---RAHLGIVSQEP---ILFDCSIAENIAYGdnsRAVSHEEIVRAAKEAnihQFIDSLpdkynTRVG-DK 1170
Cdd:PRK15134 348 PLHNLNRRQLlpvRHRIQVVFQDPnssLNPRLNVLQIIEEG---LRVHQPTLSAAQREQ---QVIAVM-----EEVGlDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1171 GT------QLSGGQKQRIAIARALVRQPHILLLDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN- 1237
Cdd:PRK15134 417 ETrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAl 492
|
250 260
....*....|....*....|...
gi 126927 1238 ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK15134 493 CHQVIVLRQGEVVEQGDCERVFA 515
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
391-617 |
2.14e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEV--QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRY 464
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 LREIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKE-----ANAYDFIMKLPHQfdtlvgergaqLSGGQK 535
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSPFE-----------LSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 613
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....
gi 126927 614 LMRE 617
Cdd:PRK13643 231 VFQE 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1051-1255 |
3.12e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQEP-ILFDCSIA 1126
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYgdnsravshEEIVRAAKEANIHQFIDSLPDKyntrVG--DKG----TQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK10908 98 DNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1201 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVIENGKVkeHGTH 1255
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1028-1249 |
3.31e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1028 LLEgnvkFNGVQFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW 1106
Cdd:PRK10535 4 LLE----LKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1107 L----RAHLGIVSQE-PILFDCSIAENIAYgdnsRAVsHEEIVRAAKEANIHQFIDSLpdKYNTRVGDKGTQLSGGQKQR 1181
Cdd:PRK10535 80 LaqlrREHFGFIFQRyHLLSHLTAAQNVEV----PAV-YAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1182 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1249
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1050-1233 |
4.08e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.65 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW---LRAH-LGIVSQ-EPILFDCS 1124
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAY----GDNSRAVSHEEIVRAAKEANIHQfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAVGLEH-----------RANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 126927 1201 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS 1233
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
391-608 |
4.88e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 95.46 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFAT-TIAENIRYGREDVT-MDEIE--KAVKEANAYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALV 545
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 546 RNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRNA--DVIAGFDGGVIVEQ 608
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIFEIcdDVTVFRDGQFIAER 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1056-1253 |
6.86e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.17 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1056 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKqlNVQWLRAHLGIVSQEPILF-DCSIAENIAYGDN 1134
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYpHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1135 SRAVSHEEIVRAAKE-ANIHQfIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEkvVQ 1213
Cdd:PRK11000 102 LAGAKKEEINQRVNQvAEVLQ-LAHLLDR-------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 126927 1214 EALDKA----REGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHG 1253
Cdd:PRK11000 172 MRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1050-1261 |
8.26e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAY-----GdnsraVSHEEIVRAAKEanihqFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:COG4152 92 LVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1202 SALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4152 158 SGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
394-616 |
9.16e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.62 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 394 KNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR-YLREIIGVV 472
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 473 SQEPVLFATTIAENI------------RYGREDvtmdeiEKAVKEANAYDFIMKLPHQfdtLVGergaQLSGGQKQRIAI 540
Cdd:PRK10575 92 QQLPAAEGMTVRELVaigrypwhgalgRFGAAD------REKVEEAISLVGLKPLAHR---LVD----SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 541 ARALVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1033-1262 |
9.75e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 9.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYP--TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQW 1106
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1107 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEIVRAAkeaniHQFIDSLPDKYNTrVGDKGTQLSGGQKQRIAI 1184
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 126927 1262 K 1262
Cdd:PRK13646 237 K 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1050-1260 |
1.21e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQ----EPilfDCSI 1125
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQfdnlDP---DFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 AENIAYGDNSRAVSHEEIvrAAKEANIHQFIdSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAA--RALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1206 TESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK13537 171 PQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
402-609 |
1.41e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVL-FA 480
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIAENIRYGRED-----VTMDE-----IEKAVKEANAYDFIMKlphQFDTlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 551 LLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 609
Cdd:PRK09536 161 LLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1051-1248 |
1.52e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 93.74 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVFLDGKEIKQLNVQWL-RAHLGIVSQEPILF-DCSIA 1126
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYGD----NSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTR-VGDKGtqlsGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:TIGR02633 97 ENIFLGNeitlPGGRMAYNAMYLRAKNL-LREL--QLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 1202 SAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:TIGR02633 170 SSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
403-585 |
1.95e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR----YLREIIGVvsqEPVL 478
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 479 fatTIAENIR-----YGREDVTMDEiekavkeanAYDFiMKLPHQFDTlvgeRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK13539 89 ---TVAENLEfwaafLGGEELDIAA---------ALEA-VGLAPLAHL----PFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 126927 554 DEATSALDTESEAVVqAALDKAREGRTTIVIA 585
Cdd:PRK13539 152 DEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
391-597 |
2.00e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLEGVVSIDGQDIRTINVRYL 465
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKST---LMKVLsgvypHGTYEGEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REI-IGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARA 543
Cdd:PRK13549 80 ERAgIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 544 LVRNPKILLLDEATSALdTESEAVVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:PRK13549 158 LNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTI 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
391-609 |
2.08e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.15 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS--------EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN- 461
Cdd:PRK10261 314 LQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 --VRYLREIIGVVSQEPvlFAT---------TIAENIRY--------GREDVTMDEIEKAVKEANAYDFimklPHQFdtl 522
Cdd:PRK10261 394 gkLQALRRDIQFIFQDP--YASldprqtvgdSIMEPLRVhgllpgkaAAARVAWLLERVGLLPEHAWRY----PHEF--- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 523 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTV-RNADVIAG 599
Cdd:PRK10261 465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAV 536
|
250
....*....|
gi 126927 600 FDGGVIVEQG 609
Cdd:PRK10261 537 MYLGQIVEIG 546
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
404-586 |
2.29e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.30 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 404 SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR---YLR-EIIGVVSQEPVLF 479
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 480 ATTIAenirygREDVTMDEIEKAVKEANAYDFIMKLPHQFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10584 101 PTLNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|...
gi 126927 556 ATSALDTES-EAVVQAALDKAREGRTT-IVIAH 586
Cdd:PRK10584 173 PTGNLDRQTgDKIADLLFSLNREHGTTlILVTH 205
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
709-979 |
2.51e-19 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 89.79 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRqncnLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 789 MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 869 GGIIEMKLLSGQAlkdKKQLEISGKIAT---EAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQA 945
Cdd:cd18552 155 PIRRIGKRLRKIS---RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMEL 231
|
250 260 270
....*....|....*....|....*....|....
gi 126927 946 MMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAV 979
Cdd:cd18552 232 LGAIAIALVLWYGGYQVISGELTPGEFISFITAL 265
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1035-1261 |
2.68e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1035 FNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQ-WLRAHLGI 1113
Cdd:PRK11288 7 FDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 VSQEPILF-DCSIAENIAYGD--NSRAVSHEEIVRA-AKEANIHQFIDSLPDkynTRVGDkgtqLSGGQKQRIAIARALV 1189
Cdd:PRK11288 84 IYQELHLVpEMTVAENLYLGQlpHKGGIVNRRLLNYeAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1190 RQPHILLLDEATSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENG-KVKEHG-----THQQL 1258
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGrYVATFDdmaqvDRDQL 233
|
...
gi 126927 1259 LAQ 1261
Cdd:PRK11288 234 VQA 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1033-1255 |
3.66e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLG 1112
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQepilFD-----CSIAEN-IAYGDNSRaVSHEEIvraakEANIHQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAI 1184
Cdd:PRK13536 118 VVPQ----FDnldleFTVRENlLVFGRYFG-MSTREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENG-KVKEHGTH 1255
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
395-597 |
4.33e-19 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 89.15 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 395 NVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtinvrylreiIGVVSQ 474
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 475 EPVLFATTIAENIRYGredVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:cd03291 106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126927 553 LDEATSALD--TESEaVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:cd03291 183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKI 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1050-1254 |
5.15e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnVQWLrahLGI-VSQEPILfdcSIAEN 1128
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL---TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 I-----AYGdnsraVSHEEIVRAAKE----ANIHQFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:COG1134 109 IylngrLLG-----LSRKEIDEKFDEivefAELGDFID-QPVKT----------YSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1200 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:COG1134 173 VLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
391-615 |
5.24e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 88.36 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRS------EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY 464
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 ----LREI-------------IGVVSQEPVLFATTIAENIRYGRedvtmdeIEKAVKE-------ANAYdfimklPHQfd 520
Cdd:COG4167 85 rckhIRMIfqdpntslnprlnIGQILEEPLRLNTDLTAEEREER-------IFATLRLvgllpehANFY------PHM-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 521 tlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:COG4167 150 ---------LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKV 220
|
250
....*....|....*...
gi 126927 598 AGFDGGVIVEQGNHDELM 615
Cdd:COG4167 221 LVMHQGEVVEYGKTAEVF 238
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1039-1261 |
5.44e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 88.36 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1039 QFNYPT----RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIV 1114
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1115 SQEPilfdcsiaeNIAYgdNSRAvsheeivraakeaNIHQFIDsLPDKYNT----------------RVG-------DKG 1171
Cdd:COG4167 93 FQDP---------NTSL--NPRL-------------NIGQILE-EPLRLNTdltaeereerifatlrLVGllpehanFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVV 1243
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLV 222
|
250
....*....|....*...
gi 126927 1244 IENGKVKEHGTHQQLLAQ 1261
Cdd:COG4167 223 MHQGEVVEYGKTAEVFAN 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
398-618 |
5.94e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 398 FNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI----------------- 460
Cdd:PRK13651 12 FNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 461 -------NVRYLREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQFDtlvgERGA-QL 530
Cdd:PRK13651 92 trfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIVIAHRLSTV--RNADVIAGFDGGVIVE 607
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIFFKDGKIIKD 246
|
250
....*....|.
gi 126927 608 QGNHDELMREK 618
Cdd:PRK13651 247 GDTYDILSDNK 257
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1049-1261 |
6.39e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGSVFLDGKEIKQLNVQWLRAHLG----IVSQEPI 1119
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 L-------FDCSIAENIAYgdnSRAVSHE----EIVRAAKEANIHQfidslpdkYNTRVGDKGTQLSGGQKQRIAIARAL 1188
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSL---HRGMRREaargEILNCLDRVGIRQ--------AAKRLTDYPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1189 VRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
391-586 |
7.59e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlreiiG 470
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQ-EPVLFATTIAENIRYGREdvtMDEIEKAVKEANAYDFIMKlphqfdtlVGERGA------QLSGGQKQRIAIARA 543
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
413-561 |
8.16e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 413 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG- 490
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 491 --------REDVTMDEIEKAVkeaNAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK10771 97 npglklnaAQREKLHAIARQM---GIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
124-336 |
8.87e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 88.34 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 124 VLIVAYIQVSLWCLAAGRQ----------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:cd18563 46 VLGLAGAYVLSALLGILRGrllarlgeriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKEL 273
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREI 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 274 ERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18563 206 KRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
391-609 |
9.19e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 86.18 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINvrylREIIG 470
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLF-ATTIAENIRY-GR-EDVTMDEIEKAVKEanaydFIMKL---PHQfdtlvGERGAQLSGGQKQRIAIARAL 544
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQlKGLKKEEARRRIDE-----WLERLelsEYA-----NKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 545 VRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 609
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
391-617 |
9.61e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.24 E-value: 9.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR---YLRE 467
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 iigvvsqEPVLFAT-TIAENIRY-GR-EDVTMDEIEKAVKEAnaydfimklphqFDTL-VGERGA----QLSGGQKQRIA 539
Cdd:COG4152 79 -------ERGLYPKmKVGEQLVYlARlKGLSKAEAKRRADEW------------LERLgLGDRANkkveELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 540 IARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1051-1258 |
9.74e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 86.27 E-value: 9.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFDCSIA-ENI 1129
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 A-----YGdNSRAVSHEEIVRAAKEANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03265 95 YiharlYG-VPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1205 DTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03265 163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
755-1251 |
1.24e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 91.01 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGaRLAVV 834
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 835 TQNVANlgtgVILSLVY----GWQLTLLLVVIIPLIVLGGIIEMKLLsgqalkdKKQLEISGKIATEAIENFRTIVSLTR 910
Cdd:COG4615 129 LQSVAL----VLGCLAYlawlSPPLFLLTLVLLGLGVAGYRLLVRRA-------RRHLRRAREAEDRLFKHFRALLEGFK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 911 EQKF-----ETMYAQSLQVP---YRNAMKKAHV-FGITFSFTQAMMYFSYAACFrfgaYLVAQQLMTFENVMLVFSAVV- 980
Cdd:COG4615 198 ELKLnrrrrRAFFDEDLQPTaerYRDLRIRADTiFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVLVLl 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 981 FGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEG--NVKFNGVQFNYPTRPNIP--VLQGLSL 1056
Cdd:COG4615 274 FLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEgfTLGPIDL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1057 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDcsiaenIAYGdnsr 1136
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------RLLG---- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1137 avsheeIVRAAKEANIHQFIDSL--PDKynTRVGDKG---TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:COG4615 424 ------LDGEADPARARELLERLelDHK--VSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRV 495
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 126927 1212 VQEAL---DKAReGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:COG4615 496 FYTELlpeLKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1050-1249 |
1.36e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.79 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAHLGIVSQEP----ILFDCS 1124
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAYGDnsravsheeivraakeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03215 95 VAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1205 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1249
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1050-1253 |
1.57e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 85.27 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPILFDcsi 1125
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 aeniaygdnsrAVSHEEIVRaakeanihqfidslpdkyNTRVGdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:cd03217 91 -----------GVKNADFLR------------------YVNEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1206 TESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHG 1253
Cdd:cd03217 137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
407-620 |
1.77e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ--DIRTINVRYLREIIGVVSQEP--VLFATT 482
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 483 IAENIRYGRED--VTMDEIEKAVKEANaydfimklphqfdTLVGERGAQ------LSGGQKQRIAIARALVRNPKILLLD 554
Cdd:PRK13638 95 IDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 555 EATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV----------RNADVIAGFDGGVIVEQGnhdELMREKGI 620
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyeisdavyvlRQGQILTHGAPGEVFACT---EAMEQAGL 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1050-1259 |
2.24e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.58 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAEN 1128
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYG--------DNSRAVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1201 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
48-336 |
2.27e-18 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 87.07 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 48 LCMILGTLAAIIhgtlLPLLMlvfGNMTDSFTKAEASILPSITNQSGPNSTLIIsnssleeemAIYAyyytgIGAgvlIV 127
Cdd:cd18547 6 ILAIISTLLSVL----GPYLL---GKAIDLIIEGLGGGGGVDFSGLLRILLLLL---------GLYL-----LSA---LF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 128 AYIQVslWCLA--AGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFII 205
Cdd:cd18547 62 SYLQN--RLMArvSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 206 GFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKN 285
Cdd:cd18547 140 MLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYK 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 126927 286 VGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18547 220 ASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVG-VIQAFLQ 269
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1031-1261 |
2.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1031 GNVKFNGVQFNYPTRP--NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG-------KEIKQ 1101
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1102 lnVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRaakeaNIHQFID--SLPDKYNTRvgdKGTQLSGG 1177
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK-----KVPELLKlvQLPEDYVKR---SPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1178 QKQRIAIARALVRQPHILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
250
....*....|....
gi 126927 1254 ------THQQLLAQ 1261
Cdd:PRK13645 234 spfeifSNQELLTK 247
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1033-1231 |
2.60e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 83.36 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikqlnvqwlraHLG 1112
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFDCSIAENIAYgdnsravsheeivraakeanihqfidslPdkyntrvgdKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY----------------------------P---------WDDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 126927 1193 HILLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1231
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
386-636 |
2.99e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.60 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 386 SIMGNLEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLydplegVVSIDGQDI------ 457
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTIvgdyai 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 458 -----RTINVRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQFdtlVGERGAQL 530
Cdd:PRK13645 76 panlkKIKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVE 607
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
250 260
....*....|....*....|....*....
gi 126927 608 QGNHDELMREKGIYFKLvmtqtrgnEIEP 636
Cdd:PRK13645 232 IGSPFEIFSNQELLTKI--------EIDP 252
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
391-613 |
3.15e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdGQdirtiNVRylreiIG 470
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFAT--TIAENIRYGREDVTmdeiekavkEANAYDFIMKL---PHQFDTLVGErgaqLSGGQKQRIAIARALV 545
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 546 RNPKILLLDEATSALDTESEAVVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFDGGVIVE-QGNHDE 613
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
388-555 |
3.50e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.47 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLRE 467
Cdd:COG1137 1 MMTLEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM-HKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 I--IGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAvKEANAY--DF-IMKLPHQfdtlvgeRGAQLSGGQKQRIAIA 541
Cdd:COG1137 77 RlgIGYLPQEASIFRKlTVEDNILAVLELRKLSKKERE-ERLEELleEFgITHLRKS-------KAYSLSGGERRRVEIA 148
|
170
....*....|....
gi 126927 542 RALVRNPKILLLDE 555
Cdd:COG1137 149 RALATNPKFILLDE 162
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
391-561 |
4.23e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTInvrylREIIG 470
Cdd:PRK11247 13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFA-TTIAENIRYGREDVTMDEIEKAVKEANAYDfimklphqfdtLVGERGAQLSGGQKQRIAIARALVRNPK 549
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPG 153
|
170
....*....|..
gi 126927 550 ILLLDEATSALD 561
Cdd:PRK11247 154 LLLLDEPLGALD 165
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1053-1258 |
4.57e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLrAHLGIVS--QEPILF-DCSIAENI 1129
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 --------------------AYgdnsRAVSHEEIVRAAkeanihQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARA 1187
Cdd:PRK11300 102 lvaqhqqlktglfsgllktpAF----RRAESEALDRAA------TWLErvGLLEHANRQAGN----LAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1188 LVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1051-1258 |
5.08e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.45 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGS-VFLDGKEIKQL-----NVQWLRAHLGIVSQEPILFD 1122
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 -CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLpdkynTRVG------DKGTQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK09984 100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1196 LLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
709-1006 |
5.28e-18 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 85.95 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrdDD--HETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRV 786
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII------DSviGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 787 RYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLI 866
Cdd:cd18542 75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 867 VLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTRE----QKFETMYAQslqvpYRNA-MKKAHVFGITFS 941
Cdd:cd18542 153 ALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREdyeiEKFDKENEE-----YRDLnIKLAKLLAKYWP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 942 FTQAMMYFSYAACFRFGAYLVAQQLMTFENvMLVFSA----VVFGAMAAGNTSSfapDYAKAKVSASHI 1006
Cdd:cd18542 228 LMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFISylwmLIWPVRQLGRLIN---DMSRASASAERI 292
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
391-617 |
5.52e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.09 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPS--RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVS-------IDGQDIRTIN 461
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 VRYLREIIGVVSQEPVLFA-TTIAENIRygrEDVTM---DEI--EKAV--------KEANAYDFIMKLPHQfdtlvgerg 527
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLelpDELarMKAVitlkmvgfDEEKAEEILDKYPDE--------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 528 aqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGV 604
Cdd:TIGR03269 428 --LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
|
250
....*....|...
gi 126927 605 IVEQGNHDELMRE 617
Cdd:TIGR03269 506 IVKIGDPEEIVEE 518
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
412-609 |
5.63e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.46 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPVLFA-TTIAENIRYG 490
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 491 REdVTMDEIEKAVKEANAYDFIMKLPHQFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQA 570
Cdd:TIGR01257 1028 AQ-LKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*....
gi 126927 571 ALDKAREGRTTIVIAHRLStvrNADVIAgfDGGVIVEQG 609
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQG 1136
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
402-585 |
5.95e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.56 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 481
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 482 TIAENIRYGREDV--TMDEIEKAVKEANaydfimkLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:TIGR01189 89 SALENLHFWAAIHggAQRTIEDALAAVG-------LTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 126927 560 LDTESEAVVQAALDkAREGRTTIVIA 585
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
145-342 |
6.77e-18 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 85.58 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 145 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLI 224
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 225 GLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLL 304
Cdd:cd18570 155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 126927 305 VYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF 342
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1040-1253 |
6.96e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.12 E-value: 6.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnVQW-LRAHLGIVSQ-- 1116
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPElt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1117 --EPILFDCSIaeniaYGdnsraVSHEEIvrAAKEANIHQFIDsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1194
Cdd:cd03220 101 grENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1195 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:cd03220 164 LLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
755-1006 |
7.03e-18 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 85.56 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKgamgarlAVV 834
Cdd:cd18551 40 ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 835 TQNVANLGTGVIL---SLV----YGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQL-EISGKIaTEAIENFRTIV 906
Cdd:cd18551 111 TSGLPQLVTGVLTvvgAVVlmflLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALgELSAAL-ERALSAIRTVK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 907 SLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQ------QLMTFenVMLVFSAVv 980
Cdd:cd18551 190 ASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASgaltvgTLVAF--LLYLFQLI- 266
|
250 260
....*....|....*....|....*.
gi 126927 981 fgaMAAGNTSSFAPDYAKAKVSASHI 1006
Cdd:cd18551 267 ---TPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1025-1258 |
7.50e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.30 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1025 KPTLLEgnVKFNGVQFN------YPTRP--NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG 1096
Cdd:PRK15079 5 KKVLLE--VADLKVHFDikdgkqWFWQPpkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1097 KEI-KQLNVQWL--RAHLGIVSQEPILF---DCSIAENIA------YGDNSRAVSHEEiVRA--AKEANIHQFIDSLPDK 1162
Cdd:PRK15079 83 KDLlGMKDDEWRavRSDIQMIFQDPLASlnpRMTIGEIIAeplrtyHPKLSRQEVKDR-VKAmmLKVGLLPNLINRYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1163 YntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-AD 1239
Cdd:PRK15079 162 F-----------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSD 230
|
250
....*....|....*....
gi 126927 1240 LIVVIENGKVKEHGTHQQL 1258
Cdd:PRK15079 231 RVLVMYLGHAVELGTYDEV 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
391-617 |
7.68e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.35 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLEGVVSIDGQDIR--TINVR 463
Cdd:cd03217 1 LEIKDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITdlPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 yLREIIGVVSQEPVLFA-TTIAENIRYgredvtmdeiekavkeanaydfimklphqfdtlVGErgaQLSGGQKQRIAIAR 542
Cdd:cd03217 75 -ARLGIFLAFQYPPEIPgVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGNhDELMRE 617
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
753-971 |
7.90e-18 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 753 FSLFFLVMGLISFVTYFFQG-----FTFGKAGeiLTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAM 827
Cdd:cd18784 35 FSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 828 GARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVS 907
Cdd:cd18784 111 SLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 908 LTREQKFETMYAQSLQVPYRNAMKKAHVFGiTFSFTQAMMYFS-YAACFRFGAYLVAQQLMTFEN 971
Cdd:cd18784 191 FANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQISGGN 254
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
391-617 |
8.96e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 8.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR-YLREII 469
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQE----PVLfatTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFD--TLVGErgaqLSGGQKQRIAIARA 543
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGF-DGGVI-----VEQGNHDELM 615
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIfALCDAITVFkDGRYVatfddMAQVDRDQLV 234
|
..
gi 126927 616 RE 617
Cdd:PRK11288 235 QA 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1045-1261 |
9.60e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.32 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-------FLDGKEIKQLNVQWLRAHLGIVSQE 1117
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1118 PILF-DCSIAENIaygdnSRAVSHEEIVRAAKEANIHQF-IDSLPDKYNTRVGDKGT-QLSGGQKQRIAIARALVRQPHI 1194
Cdd:TIGR03269 374 YDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1195 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1049-1254 |
1.07e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 89.69 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIkQLNVQWLRAHLGIVSQEPILFD-CSIAE 1127
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDNSRAVSHEEiVRAAKEANIHQfiDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-AQLEMEAMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1208 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIENGKVKEHGT 1254
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1033-1248 |
1.47e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 80.57 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErfydpmagsvfldGKeikqlnvqwLRAHLG 1112
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------------GE---------LEPDEG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILfdcsiaeNIAYgdnsravsheeivraakeanihqfidsLPdkyntrvgdkgtQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03221 56 IVTWGSTV-------KIGY---------------------------FE------------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1193 HILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
709-969 |
1.81e-17 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 84.36 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrdDDHETKRQNC----NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTK 784
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDlqglLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 785 RVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIP 864
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 865 LIVLGGIIEMKLLSGQALKDKKQL-EISGKIAtEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFT 943
Cdd:cd18544 153 LLLLATYLFRKKSRKAYREVREKLsRLNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLV 231
|
250 260
....*....|....*....|....*.
gi 126927 944 QAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18544 232 ELLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
391-618 |
2.08e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVL-FATTIAEN-IRYGRE-DVTMDEIEKAVkeANAYDFiMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 547
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 548 PKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
732-968 |
2.45e-17 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 83.93 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 732 RIVGVFSRDDDHetkrqncNLFSLFFLVMGLISFVTYFFQG-----FTFgkAGEILTKRVRYMVFKSMLRQDISWFDdhK 806
Cdd:cd18590 21 RVIDILGGEYQH-------NAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 807 NSTGSLTTRLASDASSVKGAMGARLAVVTQN-VANLGT-GVILSLvyGWQLTLLLVVIIPLIVLggIIEMKLLSGQALKD 884
Cdd:cd18590 90 TKTGDLTSRLSTDTTLMSRSVALNANVLLRSlVKTLGMlGFMLSL--SWQLTLLTLIEMPLTAI--AQKVYNTYHQKLSQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 885 KKQLEI--SGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLV 962
Cdd:cd18590 166 AVQDSIakAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLI 245
|
....*.
gi 126927 963 AQQLMT 968
Cdd:cd18590 246 QSGHLT 251
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
402-566 |
2.54e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.77 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 481
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 482 TIAENIRYGREDVTMDEIEKAVKEANAYDFimklphqFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....*
gi 126927 562 TESEA 566
Cdd:cd03231 158 KAGVA 162
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
391-615 |
2.86e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQ----EPVLfatTIAENIR-YGRE-DVTMDEIEKAVkeANAYDFiMKLPHQFDTLVGErgaqLSGGQKQRIAIARAL 544
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
752-992 |
3.76e-17 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 83.30 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 752 LFSLFFLVMGLISFVTYFFqgftFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 832 AVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGII---EMKLLSGQAlKDKkqLEISGKIATEAIENFRTIVSL 908
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 909 TREQKFETMYAQSLQVPYRNAMKKAHvfgitfsftqammyfsyaacfrfgaylvAQQLMTFENVMLVFSAVVF------- 981
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRRIR----------------------------ARALLTALVIFLVFGAIVFvlwlgah 243
|
250
....*....|....*
gi 126927 982 ----GAMAAGNTSSF 992
Cdd:cd18575 244 dvlaGRMSAGELSQF 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
397-584 |
3.84e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.38 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 397 HFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIiGVV--SQ 474
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI-GVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 475 EPVLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:cd03267 104 TQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190
....*....|....*....|....*....|...
gi 126927 553 LDEATSALDTESEAVVQAALDKA-REGRTTIVI 584
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL 209
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
765-973 |
4.27e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 83.36 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 765 FVTYFFQG-FTF------GKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGarlAVVTQN 837
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTADVQEFKSSFK---QCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 838 VANLG--TGVILSLVY-GWQLTLLLVVIIPLIVLGGII---EMKLLSGQAlkdKKQLEISGKIATEAIENFRTIVSLTRE 911
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLygsFLRKLSRRA---QAQVAKATGVADEALGNIRTVRAFAME 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 912 QKFETMYAQSLQvpyrNAMKKAHVFGITFSFTQAMMYFS---------YaacfrFGAYLVAQQLMTFENVM 973
Cdd:cd18574 201 DRELELYEEEVE----KAAKLNEKLGLGIGIFQGLSNLAlngivlgvlY-----YGGSLVSRGELTAGDLM 262
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1044-1251 |
4.45e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGSVFLDGKE-----IKQlnvqwlRAHLGIV- 1114
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVcrfkdIRD------SEALGIVi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1115 -SQE----PILfdcSIAENIAYGdNSRA----VSHEEIVRAAKE--ANIhqfidSLPDKYNTRVGDKGTqlsgGQKQRIA 1183
Cdd:NF040905 83 iHQElaliPYL---SIAENIFLG-NERAkrgvIDWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1184 IARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKE 1251
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1049-1249 |
4.84e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAHLGIVS----QEPILFDC 1123
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYGdNSRAVSHEEIVRAAKEANI-HQFIDSLpdkyNTRVGDKGT---QLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:COG1129 346 SIRENITLA-SLDRLSRGGLLDRRRERALaEEYIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1200 ATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1249
Cdd:COG1129 421 PTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1033-1264 |
5.24e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.85 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerFYDPMA--GSVFLDGKEIKQL-NVQWLRA 1109
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWqTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILFD-CSIAENIAYGD--NSRAVSHEEIVRAakeanihqfIDSLPDKYNTRVGDKGTqLSGGQKQRIAIAR 1186
Cdd:PRK11614 81 AVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAIGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1187 ALVRQPHILLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
...
gi 126927 1262 KGI 1264
Cdd:PRK11614 228 EAV 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
391-586 |
8.33e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.64 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYLreiig 470
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 vvsqepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 126927 551 LLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 586
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
407-614 |
9.13e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLMQRLYDP----LEGVVSIDGQDIRTINVRYLREI----IGVVSQEPV 477
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 478 LFAT---TIAENI-------RYGREDVTMDE---------IEKAVKEANAYdfimklPHQfdtlvgergaqLSGGQKQRI 538
Cdd:PRK15134 103 VSLNplhTLEKQLyevlslhRGMRREAARGEilncldrvgIRQAAKRLTDY------PHQ-----------LSGGERQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
403-614 |
9.18e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDPLE--GVVSIDGqdiRTINVRYLREIIGVVSQEPVLF 479
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVKgsGSVLLNG---MPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 480 AT-TIAENI------RYGReDVTMDEIEKAVKEanaydFI--MKLPHQFDTLVGERGAQ--LSGGQKQRIAIARALVRNP 548
Cdd:TIGR00955 112 PTlTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 549 KILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLST--VRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
391-614 |
9.79e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFAT-TIAENIRYG--REDVTMDEIEKAVKEANAYdfiMKLPHQFDTL-VGERgaqlsggqkQRIAIARALV 545
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 546 RNPKILLLDEATSALD-TESEAV---VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1048-1249 |
1.04e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeiKQLNVQWLRAH-LGI--VSQEPILF-DC 1123
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqLGIylVPQEPLLFpNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1204 LD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:PRK15439 171 LTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1033-1258 |
1.20e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFnypTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RA 1109
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQfidslpdkyntrVGDKG------TQLSGGQKQRI 1182
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA------------VGLRGaaklmpSELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1183 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1044-1229 |
1.62e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQ-EPILfd 1122
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 cSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK13539 89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*..
gi 126927 1203 ALDTESEKVVQEALdKAREGRTCIVIA 1229
Cdd:PRK13539 157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
145-329 |
1.95e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 81.44 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 145 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVskindgiGDKIGMFFQSITTFLAGF--IIG------FISGwKLTLV 216
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV-------QEFKSSFKQCVSQGLRSVtqTVGcvvslyLISP-KLTLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 217 ILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKN--------VGI 288
Cdd:cd18574 148 LLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKlneklglgIGI 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126927 289 KKAITaSISIGIAYLLVYasyalafWYGTSLVLSNEYSIGE 329
Cdd:cd18574 228 FQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGD 260
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
408-615 |
2.27e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFA-TTIAEN 486
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 487 IRYGREDVT------MDEIEKAVKEANAYDFIMKLPHQ-FDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10253 102 VARGRYPHQplftrwRKEDEEAVTKAMQATGITHLADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 560 LDTESEA-VVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK10253 174 LDISHQIdLLELLSELNREkGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1045-1259 |
3.16e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGSVFLDGKEIkqlNVQWLRAHLGIVSQEPIL 1120
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1121 FDCSIA-ENIAYgdNSRAVSHEEIVRAAKEANIHQFID--SLPDKYNTRVGDKGTQ--LSGGQKQRIAIARALVRQPHIL 1195
Cdd:TIGR00955 111 IPTLTVrEHLMF--QAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1196 LLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1049-1254 |
3.53e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.74 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP-ILFDCSIAE 1127
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENhINSRLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYG------------DnsravshEEIVRAAkeanIHQF-IDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHI 1194
Cdd:COG4604 95 LVAFGrfpyskgrltaeD-------REIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1195 LLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIENGKVKEHGT 1254
Cdd:COG4604 157 VLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
408-589 |
4.30e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.09 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI----IGVVSQEPVLFATTI 483
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AenirygREDVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK11629 104 A------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 126927 562 TESEAVVQAALDK--AREGRTTIVIAHRLS 589
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1045-1258 |
4.31e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG-------------KEIKQLNVQWLR-AH 1110
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1111 LGIVSQEPI-----LFDC--SIAENIAYgdnSRAVSHEEIVRAAKeanihQFIDS--LPDKyNTRVGDKGTQLSGGQKQR 1181
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRL---HQGASREEAMVEAK-----RMLDQvrIPEA-QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1182 IAIARALVRQPHILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
....*
gi 126927 1254 THQQL 1258
Cdd:PRK10261 252 SVEQI 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
407-602 |
4.53e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI---RTINVRYLREIIGVVSQE-------- 475
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhhllmdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 476 -------PVLFATTIAENIRYgREDVTMDEIEKAVKEANaydfimkLPhqfdtlvgergAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK10908 96 vydnvaiPLIIAGASGDDIRR-RVSAALDKVGLLDKAKN-------FP-----------IQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 549 KILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV--RNADVIAGFDG 602
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsrRSYRMLTLSDG 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
388-610 |
5.48e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR-YLR 466
Cdd:PRK10895 1 MATLTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 EIIGVVSQEPVLFAT-TIAENIRYG---REDVTMDEIEKAVKEANAyDFimKLPHQFDTLvgerGAQLSGGQKQRIAIAR 542
Cdd:PRK10895 78 RGIGYLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELME-EF--HIEHLRDSM----GQSLSGGERRRVEIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRlsTVRnaDVIAGFDGGVIVEQGN 610
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH--NVR--ETLAVCERAYIVSQGH 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1050-1216 |
7.70e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.53 E-value: 7.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI 1129
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 AY--GDNSRavshEEIVRAAKEANIHQFIDsLPdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 126927 1208 SEKVVQEAL 1216
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
406-592 |
8.13e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-IGVVSQE-PVLFATTI 483
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AENIRYGRE------DVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK09700 98 LENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 126927 558 SALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVR 592
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIR 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1046-1248 |
9.43e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 9.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-------QlnvqwlRAHLGIVSQEP 1118
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssQ------EAGIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILFD-CSIAENIAYGdnsravshEEIVRAAKEAN---IHQFIDSLPDKYN------TRVGDkgtqLSGGQKQRIAIARAL 1188
Cdd:PRK10762 89 NLIPqLTIAENIFLG--------REFVNRFGRIDwkkMYAEADKLLARLNlrfssdKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1189 VRQPHILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENGK 1248
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1049-1229 |
1.43e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.63 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYgdnsravsheeivraakEANIHQFIDSLPDKYNTRVGDKG------TQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:TIGR01189 94 LHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*..
gi 126927 1203 ALDTESEKVVQEALDkAREGRTCIVIA 1229
Cdd:TIGR01189 157 ALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
395-616 |
1.54e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 395 NVHFNYpSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN--VRYLREI---- 468
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 --------IGVVSQEPV-----LFAT--TIAENIR----YGREDvtmdeiekAVKEANAYDFIMKLPhQFDTLVGERGAQ 529
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREE--------AMVEAKRMLDQVRIP-EAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------VVQAALDKAregrtTIVIAHRLSTVRN-ADVIAGFD 601
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqlikVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMY 243
|
250
....*....|....*
gi 126927 602 GGVIVEQGNHDELMR 616
Cdd:PRK10261 244 QGEAVETGSVEQIFH 258
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
391-609 |
2.05e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 76.13 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPS-RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDPL-EGVVSIDGQDIRtinvRYLRE 467
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEPVLFAT-TIAENIRygredvtmdeiekavkeanaydFIMKLphqfdtlvgeRGaqLSGGQKQRIAIARALVR 546
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 547 NPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFDGGVIVEQG 609
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
391-560 |
2.49e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-NVRYLREII 469
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFA-TTIAENIRYGREDVTMDEIEKAVKEAnaYDFimkLPHQFDTLVgERGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 126927 549 KILLLDEATSAL 560
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
392-601 |
2.85e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 81.69 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRSEV-QILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRLYDPLEGVVSIDGqdIRTINVRYLRE--- 467
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGG--DRLVNGRPLDSsfq 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 -IIGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKavKEANAY-DFIMKL---PHQFDTLVGERGAQLSGGQKQRIAIA 541
Cdd:TIGR00956 836 rSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIG 913
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 542 RALVRNPKILL-LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFD 601
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFD 971
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
50-344 |
3.42e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 77.99 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 50 MILGTLAAIIhGTLLPLL-MLVFGNMTDSFTKAEASILPSITNQSGPNSTliisnsslEEEMAIYAYYYTGIGAGVLIVA 128
Cdd:cd18565 1 LVLGLLASIL-NRLFDLApPLLIGVAIDAVFNGEASFLPLVPASLGPADP--------RGQLWLLGGLTVAAFLLESLFQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 129 YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFI 208
Cdd:cd18565 72 YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 209 SGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEE--AKNV 286
Cdd:cd18565 152 LNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEyrDANW 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 287 GikkAITASIS-IGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVffsillGTFSI 344
Cdd:cd18565 232 R---AIRLRAAfFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
399-617 |
4.93e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 399 NYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGqdirtiNVRYLREIIGVVSQEpvl 478
Cdd:COG1134 32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLELGAGFHPE--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 479 faTTIAENIR-----YGredVTMDEIEKAVKEANAY----DFImklphqfDTLVGergaQLSGGQKQRIAIARALVRNPK 549
Cdd:COG1134 103 --LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPVK----TYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 550 ILLLDEATSALDTE----SEAVVQaalDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG1134 167 ILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1047-1249 |
5.67e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGSVFLDGKEIKQLNVQWLRAH-LGIVSQEP----- 1118
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrgl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILfDCSIAENIAYGD-NSRAVSHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGT---QLSGGQKQRIAIARALVRQPHI 1194
Cdd:COG3845 348 VP-DMSVAENLILGRyRRPPFSRGGFLDRKA---IRAFAEELIEEFDVRTPGPDTparSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1195 LLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1050-1270 |
5.74e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.46 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQWLRAHLG---------IVSQEP 1118
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPSKVGepcpvcggtLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILFDCS------IAENIA---------YGDNSRAV----SHEEIVRAAKEAnIHQFIDSLPD-KYNTRVGDKGTQLSGGQ 1178
Cdd:TIGR03269 95 DFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1179 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTH 1255
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTP 253
|
250
....*....|....*
gi 126927 1256 QQLLAQKGIYFSMVQ 1270
Cdd:TIGR03269 254 DEVVAVFMEGVSEVE 268
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1027-1260 |
5.99e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1027 TLLEgnVKFNGVQFNYPT----RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQL 1102
Cdd:PRK15112 3 TLLE--VRNLSKTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1103 NVQWLRAHLGIVSQEPI-----------LFDCSIAENIAYGDNSRAvshEEIVRAAKEANIhqfidsLPDKYNTRvgdkG 1171
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQRE---KQIIETLRQVGL------LPDHASYY----P 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:PRK15112 148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGE 227
|
250
....*....|..
gi 126927 1249 VKEHGTHQQLLA 1260
Cdd:PRK15112 228 VVERGSTADVLA 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-614 |
7.73e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGV-----VSIDGQDIRTI-NVRYLREIIGVVSQEPVLFAT 481
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 482 TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 562 TESEAVVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
391-606 |
8.34e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKN--VHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTV-QLMQRLYDP--LEGVVSIDGQDIRTINVRYL 465
Cdd:PRK09473 13 LDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfALMGLLAANgrIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REI----IGVVSQEPVlfaTTIAENIRYG-------------------REDVTMDEiekAVKEANAYDFIMKLPHQFdtl 522
Cdd:PRK09473 92 NKLraeqISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmskaeafEESVRMLD---AVKMPEARKRMKMYPHEF--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 523 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGF 600
Cdd:PRK09473 163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGI 228
|
....*.
gi 126927 601 DGGVIV 606
Cdd:PRK09473 229 CDKVLV 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1040-1253 |
8.56e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1040 FNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQ 1116
Cdd:PRK10261 330 LNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1117 EPIlfdCSIAENIAYGDnsravSHEEIVRaakeanIHQFIDSLPDKYNT-----RVGDKGT-------QLSGGQKQRIAI 1184
Cdd:PRK10261 409 DPY---ASLDPRQTVGD-----SIMEPLR------VHGLLPGKAAAARVawlleRVGLLPEhawryphEFSGGQRQRICI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1185 ARALVRQPHILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:PRK10261 475 ARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
709-969 |
1.03e-14 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 76.29 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNCNLFS--LFFLVMGLISFVTYFFQGFTFGKAGEILTKRV 786
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRilLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 787 RYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLI 866
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 867 VLGgiieMKLLSGQALKD-KKQLEISGKI---ATEAIENFRTIVSLTRE----QKFETMYAQslqvpYRNAMKKAHVF-G 937
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEINEE-----LYKASFKAQFYsG 229
|
250 260 270
....*....|....*....|....*....|..
gi 126927 938 ITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18547 230 LLMPIMNFINNLGYVLVAVVGGLLVINGALTV 261
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
407-561 |
1.11e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVK-----SGQTvALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ---DI-RTINVRYLREIIGVVSQEPV 477
Cdd:PRK11144 8 QQLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 478 LFA-TTIAENIRYGredvtMDEIEKAvkeanaydfimklphQFDTLVGERG---------AQLSGGQKQRIAIARALVRN 547
Cdd:PRK11144 87 LFPhYKVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTA 146
|
170
....*....|....
gi 126927 548 PKILLLDEATSALD 561
Cdd:PRK11144 147 PELLLMDEPLASLD 160
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
406-597 |
1.11e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.29 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLEGVVSIDGQ-----DIRTinvrylREIIGVV--S 473
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD------SEALGIViiH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 474 QE----PVLfatTIAENIRYGREDVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAqlsgGQKQRIAIARALVRN 547
Cdd:NF040905 85 QElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 126927 548 PKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
114-555 |
1.49e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 78.30 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 114 AYYYTGIGAGVLIVAYIQvslwclaagRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDkIGMFF 193
Cdd:COG4615 60 LLLLSRLASQLLLTRLGQ---------HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFLAGFI-IGFISgWKLTLVILAVSPLIGLSSALwakvLTSFTNKELQayaKAGAVAEEVLAAIRTVIafGGQqKE 272
Cdd:COG4615 130 QSVALVLGCLAyLAWLS-PPLFLLTLVLLGLGVAGYRL----LVRRARRHLR---RAREAEDRLFKHFRALL--EGF-KE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 273 L------------ERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNeysiGEVLTVFFSILLg 340
Cdd:COG4615 199 LklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWAD----PAVLSGFVLVLL- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 341 tFSIGHLAP---NIEAFANARgAAFEifKI------IDNEPSIDSFSTKGyKPDSIMGNLEFKNVHFNYPSRSEVQ--IL 409
Cdd:COG4615 274 -FLRGPLSQlvgALPTLSRAN-VALR--KIeelelaLAAAEPAAADAAAP-PAPADFQTLELRGVTYRYPGEDGDEgfTL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 410 KGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTiaenirY 489
Cdd:COG4615 349 GPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------L 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 490 GREDVTMDEiekavkEANAYDFIMKLPH-------QFDTLvgergaQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG4615 423 GLDGEADPA------RARELLERLELDHkvsvedgRFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
376-609 |
1.56e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 74.11 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 376 SFSTKGYKPDSIMgnleFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ 455
Cdd:cd03220 9 SYPTYKGGSSSLK----KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 456 dirtinVRYLREI-IGVvsqEPVLfatTIAENIR-----YGREDVTMDEIEKAVKE-ANAYDFImklphqfDTLVGErga 528
Cdd:cd03220 85 ------VSSLLGLgGGF---NPEL---TGRENIYlngrlLGLSRKEIDEKIDEIIEfSELGDFI-------DLPVKT--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 529 qLSGGQKQRIAIARALVRNPKILLLDEATSALDtesEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGG 603
Cdd:cd03220 143 -YSSGMKARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQRRLREllkqGKTVILVSHDPSSIKRlCDRALVLEKG 218
|
....*.
gi 126927 604 VIVEQG 609
Cdd:cd03220 219 KIRFDG 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1051-1247 |
1.63e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLG--IVSQEPILFD-CSIAE 1127
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDN-SRAVSHEEIVRAAK---EANIHQFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK09700 100 NLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 126927 1204 L-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENG 1247
Cdd:PRK09700 176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
391-615 |
1.71e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVH--FNYPS----RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY 464
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 465 LREIIGVVSQEPvlfATTIAENIRYGR---------EDVTMDEIEKAVKE-----------ANAYdfimklPHQfdtlvg 524
Cdd:PRK15112 85 RSQRIRMIFQDP---STSLNPRQRISQildfplrlnTDLEPEQREKQIIEtlrqvgllpdhASYY------PHM------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 525 ergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFD 601
Cdd:PRK15112 150 -----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMH 224
|
250
....*....|....
gi 126927 602 GGVIVEQGNHDELM 615
Cdd:PRK15112 225 QGEVVERGSTADVL 238
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1035-1261 |
2.00e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.70 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1035 FNGVQFNYPTrPNIPVlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIV 1114
Cdd:PRK10522 325 LRNVTFAYQD-NGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1115 SQEPILFDcsiaeniaygdnsRAVSHEEivRAAKEANIHQFIDSLPDKYNTRVGD---KGTQLSGGQKQRIAIARALVRQ 1191
Cdd:PRK10522 403 FTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1192 PHILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE-HGTHQQLLAQ 1261
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1051-1259 |
2.11e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.58 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL----RAHL-----GIVSQEP--- 1118
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILFDCSIAENI-----AYGDNsravsHEEIVRAAKEANIHQF-IDSlpdkynTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:PRK11701 102 LRMQVSAGGNIgerlmAVGAR-----HYGDIRATAGDWLERVeIDA------ARIDDLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1193 HILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK11701 171 RLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
406-634 |
2.28e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.56 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLY--DPLEGVVSIDGQDIRTINVRYL-REIIGVVSQEPVLFAT- 481
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 482 TIAENIRYGRE----DVTMDEIEkAVKEANAYDFIMKLPHQFDTL-VGERGaqlsGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:TIGR02633 94 SVAENIFLGNEitlpGGRMAYNA-MYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 557 TSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRnadviAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEI 634
Cdd:TIGR02633 169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREI 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
406-638 |
2.35e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.54 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRL--YDPLEGVV----------------SIDGQ------------ 455
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 456 --DIRTINVRYLREIIGVVSqepVLFATTIAeniRYGREDV------TMDEIEKAVKEA--NAYDFI--MKLPHQFDTLV 523
Cdd:TIGR03269 93 evDFWNLSDKLRRRIRKRIA---IMLQRTFA---LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 524 GErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIAGF 600
Cdd:TIGR03269 167 RD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWL 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 126927 601 DGGVIVEQGNHDELMrekGIYFKLVMTQTRGNEIEPGN 638
Cdd:TIGR03269 243 ENGEIKEEGTPDEVV---AVFMEGVSEVEKECEVEVGE 277
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1025-1259 |
3.30e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1025 KPTLLEGNVKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV 1104
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1105 QWLRAHLGIVSQE-PILFDCSIAENIA------------YGDNSRAVSHEEIVRAAKEANIHQFIDSlpdkyntrvgdkg 1171
Cdd:PRK10575 81 KAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1172 tqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIENG 1247
Cdd:PRK10575 148 --LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGG 224
|
250
....*....|..
gi 126927 1248 KVKEHGTHQQLL 1259
Cdd:PRK10575 225 EMIAQGTPAELM 236
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
109-332 |
3.94e-14 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 74.43 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 109 EMAIYayYYTG--------------IGAGVLIVAYIQVS----------LWCLAAGRQIHKIRQKFFHAIMNQEIGWFDV 164
Cdd:cd18589 12 EMAIP--YYTGrmtdwimnkdapeaFTAAITVMSLLTIAsavsefvcdlIYNITMSRIHSRLQGLVFAAVLRQEIAFFDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 165 HDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQ 244
Cdd:cd18589 90 NQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 245 AYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNE 324
Cdd:cd18589 170 SLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGT 249
|
....*...
gi 126927 325 YSIGEVLT 332
Cdd:cd18589 250 VSSGDLVT 257
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1048-1249 |
4.06e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.52 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlNVQW-----LRAHLGIV--SQEPIL 1120
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1121 FDCSIAENIAYgdnsravsHEEIVRAaKEANIHQFIDSLPDKYN-TRVGDKGT-QLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:cd03267 108 WDLPVIDSFYL--------LAAIYDL-PPARFKKRLDELSELLDlEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 1199 EATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
418-610 |
5.14e-14 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 70.87 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 418 SGQTVALVGNSGCGKSTTVQ-LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIgvvsqepvlfattiaenirygredvtm 496
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 497 deiekavkeanaydfimklphqfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--- 573
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126927 574 ----KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 610
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
397-587 |
6.35e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 397 HFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLY--DPLEGVVSIDGQDIrtinvrylreiigvvS 473
Cdd:COG2401 33 AFGVELRVvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 474 QEpvlfaTTIAENIryGREDVTMDEIE--KAVKEANAYDFIMKLPHqfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:COG2401 98 RE-----ASLIDAI--GRKGDFKDAVEllNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 126927 552 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIA-HR 587
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
146-342 |
7.79e-14 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 73.59 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 146 IRQKFFHAIMNqeigwFDVHDVGE-----LNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAV 220
Cdd:cd18548 74 LRKDLFEKIQS-----FSFAEIDKfgtssLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 221 SPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:cd18548 149 IPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 301 AYLLVYASYALAFWYGTSLVLSNEYSIGEV-------LTVFFSILLGTF 342
Cdd:cd18548 229 MMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1047-1254 |
7.85e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPIlfd 1122
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflAFQYPI--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 cSIAeniaygdnsrAVSHEEIVRAA----------KEANIHQFIDSLPDKYNTrVGDKGTQL--------SGGQKQRIAI 1184
Cdd:CHL00131 95 -EIP----------GVSNADFLRLAynskrkfqglPELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1054-1253 |
8.60e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.53 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1054 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-DC 1123
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYG-DNSRAVSHEEIVRAAKeanihqfIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK11144 92 KVRGNLRYGmAKSMVAQFDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 1203 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:PRK11144 158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
143-340 |
9.60e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 73.29 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 143 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSP 222
Cdd:cd18550 71 MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 223 LIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAA--IRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:cd18550 151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 126927 301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLG 340
Cdd:cd18550 231 LGLFTAIGPALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1014-1233 |
1.01e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 75.94 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1014 PEIDSYSTEGLKPTLLEGN----VKFNGVQF-NYP--TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD 1086
Cdd:TIGR00954 424 EEIESGREGGRNSNLVPGRgiveYQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1087 PMAGSVFLDGKeikqlnvqwlrAHLGIVSQEPILFDCSIAENIAYGDNS-----RAVSHEEIVRAAKEANIHQFIdslpd 1161
Cdd:TIGR00954 504 VYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLEQILDNVQLTHIL----- 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1162 kynTR------VGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1233
Cdd:TIGR00954 568 ---EReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
393-585 |
1.02e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 71.14 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 393 FKNVHFNYP-SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL------YDPLEGVVSIDGQDIRTINVRYL 465
Cdd:cd03233 6 WRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 466 REIIgVVSQEPVLFAT-TIAEnirygredvTMDeiekAVKEANAYDFImklphqfdtlvgeRGaqLSGGQKQRIAIARAL 544
Cdd:cd03233 83 GEII-YVSEEDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEAL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 126927 545 VRNPKILLLDEATSALDTESeavvqaALD-------KAREGRTTIVIA 585
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSST------ALEilkcirtMADVLKTTTFVS 175
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1050-1264 |
1.37e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPilfdcSIAE 1127
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEA-----SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDNSRAV--------SHEEIVRAAK---EANIHQFIDSLpdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:PRK10895 92 RLSVYDNLMAVlqirddlsAEQREDRANElmeEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1197 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLAQKGI 1264
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
409-603 |
1.42e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 70.15 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-IGVVSQEPV---LFAT-TI 483
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AENIrygredvtmdeiekavkeanaydfimklphqfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 126927 564 SEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGG 603
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1044-1249 |
1.59e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.77 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-----------VQWLRAHLG 1112
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 IVSQEPILFDCSIAENIAYGDNSRAVSHEEIvraakEANIHQFIDSLPDK---YNTRVGdkgtQLSGGQKQRIAIARALV 1189
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1190 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
397-616 |
1.86e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 397 HFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDP-------LEGVVSIDGQDIRTINVRYLREI 468
Cdd:PRK13547 6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQ--EPVlFATTIAENIRYGR----------EDVTMDEIEKAVKEANAydfimklphqfDTLVGERGAQLSGGQKQ 536
Cdd:PRK13547 85 RAVLPQaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 537 RIAIARAL---------VRNPKILLLDEATSALDTESE----AVVQAALDKAREGRTTIVIAHRLSTvRNADVIAGFDGG 603
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADG 231
|
250
....*....|...
gi 126927 604 VIVEQGNHDELMR 616
Cdd:PRK13547 232 AIVAHGAPADVLT 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
412-617 |
2.16e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYdPLEGVVSIDGQDIRTINVRYLREIIGVVSQE-PVLFATTIAENI-RY 489
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLtLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 490 GREDVTMDEIEKAVKE-ANAYDFIMKLPhqfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSALD 561
Cdd:PRK03695 94 QPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 562 TESeavvQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK03695 166 VAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
408-616 |
2.33e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP----LEGVVSIDGQDIRTINVRylREIIGVVSQEP------- 476
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPrsafnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 477 VLFATTIAENIR-YGRE--DVTMDEIEKAVKEANAyDFIMKLpHQFdtlvgergaQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK10418 96 HTMHTHARETCLaLGKPadDATLTAALEAVGLENA-ARVLKL-YPF---------EMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 554 DEATSALDteseAVVQA-ALD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK10418 165 DEPTTDLD----VVAQArILDllesiVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
117-334 |
2.72e-13 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 72.12 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 117 YTGIGAGVLIVAYIQVSLWCLAAGRQ----------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIG 186
Cdd:cd18545 36 LSGLLIIALLFLALNLVNWVASRLRIylmakvgqriLYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 187 DKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAF 266
Cdd:cd18545 116 NGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSF 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 267 GGQQKELERYNKNLEEAKNVGIKKAITASI---SIGIAYLLvyaSYALAFWYGTSLVLSNEYSIGeVLTVF 334
Cdd:cd18545 196 AREDENEEIFDELNRENRKANMRAVRLNALfwpLVELISAL---GTALVYWYGGKLVLGGAITVG-VLVAF 262
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
391-611 |
4.08e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.59 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKST-TVQLMQRL-YDPLEGVVSIDGQDIRTIN------- 461
Cdd:PRK09580 2 LSIKDLHV---SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 -----VRYLREIIGVVSQepvLFATTIAENIRYGREDVTMDEIEKAvkeanayDFI------MKLPHqfDTLVGERGAQL 530
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFDGGVIVE 607
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
....
gi 126927 608 QGNH 611
Cdd:PRK09580 227 SGDF 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1049-1231 |
4.67e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVFLDGKEIKQlnvqwlrahlgivsqepilfDCSIA 1126
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIA-YGDNSRAVsheEIVRAAKeanihqfidsLPDKYNTRVgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:COG2401 104 DAIGrKGDFKDAV---ELLNAVG----------LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*...
gi 126927 1206 TESEKVVQEALDKA--REGRTCIVIAHR 1231
Cdd:COG2401 169 RQTAKRVARNLQKLarRAGITLVVATHH 196
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
755-1006 |
4.68e-13 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 71.28 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGA--MGARLA 832
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 833 VVTqnVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTRE- 911
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 912 ---QKFETMYAQslqvpYRNAMKKA-HVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFS---AVVFGAM 984
Cdd:cd18548 199 yeeERFDKANDD-----LTDTSLKAgRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINylmQILMSLM 273
|
250 260
....*....|....*....|..
gi 126927 985 AAGNTSSFAPdyaKAKVSASHI 1006
Cdd:cd18548 274 MLSMVFVMLP---RASASAKRI 292
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1049-1253 |
8.23e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.73 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQlnvQWLRA-HLGIVSQEP----- 1118
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRGrKIATIMQNPrsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ---ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK10418 94 plhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 1196 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
118-339 |
1.18e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 70.20 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 118 TGIGAGVLIVAYIQvslWCLAAGRQI----------HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGd 187
Cdd:cd18543 39 WPLVLLLLALGVAE---AVLSFLRRYlagrlslgveHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 188 KIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTnkeLQAYAKAGAVA---EEVLAAIRTVI 264
Cdd:cd18543 115 FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVK 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 265 AFGGQQKELERYNKNLEEAKNVGIKKA-ITASISIGIAyLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFSILL 339
Cdd:cd18543 192 AFGRERRELDRFEAAARRLRATRLRAArLRARFWPLLE-ALPELGLAAVLALGGWLVANGSLTLGT-LVAFSAYLT 265
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
391-614 |
1.21e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYL---RE 467
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IIGVVSQEPVLFA-TTIAENIRYG-REDVTMDE--IEKAVkeanaydfIMKLphqfdTLVGERGA------QLSGGQKQR 537
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKL-----EAVGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHR----LSTVRNADVIAGFDggvIVEQGNH 611
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVADKK---IVAHGSA 228
|
...
gi 126927 612 DEL 614
Cdd:PRK11831 229 QAL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-618 |
1.25e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHfnYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:COG3845 258 LEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVVSQEPVLFAT----TIAENI---RYGREDVT------MDEIEKAVKEA-NAYDfiMKLPHQfDTLVGergaQLSGGQK 535
Cdd:COG3845 336 AYIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEELiEEFD--VRTPGP-DTPAR----SLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 613
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAE 488
|
....*
gi 126927 614 LMREK 618
Cdd:COG3845 489 ATREE 493
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
388-591 |
1.35e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNL-EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtinvryLR 466
Cdd:PRK09544 1 MTSLvSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 eiIGVVSQEPVLFAT---TIAENIRYgREDVTMDEIEKAVKEANAYDFImKLPHQfdtlvgergaQLSGGQKQRIAIARA 543
Cdd:PRK09544 69 --IGYVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTV 591
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1043-1260 |
1.39e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.78 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGSVFLDGKEIKQLN-VQWLRAHLGIVSQEP-- 1118
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 --ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLpdKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1196 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK----EHG-THQQLLA 1260
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
709-968 |
1.42e-12 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 69.75 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIV-GVFSRDDDHETKRQNCnlfsLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVR 787
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIdALTAGTLTASQLLRYA----LLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 788 YMVFKSMLRQDISWFddHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIV 867
Cdd:cd18541 77 NDLFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 868 LGGIIEMKLLSGQALKDKKQLeisGKIATEAIENF---RTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQ 944
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAF---SDLSDRVQESFsgiRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
|
250 260
....*....|....*....|....
gi 126927 945 AMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18541 232 LLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1043-1260 |
1.55e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGSVFLDGKEIKQLN-VQWLRAHLGIVSQEP-- 1118
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 --ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNT---RVGdkgtQLSGGQKQRIAIARALVRQPH 1193
Cdd:PRK13549 350 dgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1194 ILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK-----EHGTHQQLLA 1260
Cdd:PRK13549 426 ILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlinHNLTQEQVME 499
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
411-586 |
1.68e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 411 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREII------GVvsqEPVLfatTIA 484
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 485 ENIRY-------GREDVTMDEIEKavkeanaydfimklphqfdtlVGERG------AQLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK13538 93 ENLRFyqrlhgpGDDEALWEALAQ---------------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 126927 552 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAH 586
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
407-603 |
2.26e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRL----------YDPLEGVVSIDGQDIRtiNVRYLREIIGVVSQEP 476
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLAR--DIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 477 VLF-ATTIAENIRYGREDVT------MDEIEKAVKEaNAYDFIMK--LPHqfdtLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK09984 96 NLVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRvgMVH----FAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 548 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAH----------RLSTVRNADVIagFDGG 603
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHqvdyalryceRIVALRQGHVF--YDGS 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
390-617 |
2.30e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 390 NLEFKNVHF---NYPSRSEVQIlkglNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLEGVVS-----IDGQDIRTIN 461
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 VRYLREIIG----VVSQEPVlfaTTIAENIRYGREdvTMDEIE------KAVKEANAYDFImklphqfdTLVG-----ER 526
Cdd:PRK11022 80 EKERRNLVGaevaMIFQDPM---TSLNPCYTVGFQ--IMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 527 ----GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTV-RNADVIAG 599
Cdd:PRK11022 147 ldvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAqIIELLLElQQKENMALVLITHDLALVaEAAHKIIV 226
|
250
....*....|....*...
gi 126927 600 FDGGVIVEQGNHDELMRE 617
Cdd:PRK11022 227 MYAGQVVETGKAHDIFRA 244
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1032-1261 |
3.32e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1032 NVKFNGVQFNYPTrPNIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGSVFLDGKEI-----KQLN 1103
Cdd:PRK09473 14 DVKDLRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlnlpeKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1104 VqwLRA-HLGIVSQEPIlfdCSIAENIAYGDN-----------SRAVSHEEIVR---AAKEANIHQFIDSLPDKYntrvg 1168
Cdd:PRK09473 93 K--LRAeQISMIFQDPM---TSLNPYMRVGEQlmevlmlhkgmSKAEAFEESVRmldAVKMPEARKRMKMYPHEF----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1169 dkgtqlSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIE 1245
Cdd:PRK09473 163 ------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMY 236
|
250
....*....|....*.
gi 126927 1246 NGKVKEHGTHQQLLAQ 1261
Cdd:PRK09473 237 AGRTMEYGNARDVFYQ 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
409-591 |
3.72e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRtinvRYLRE-IIGVVSQE-------PVLFA 480
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIAENiRYG-----REDVTMDEieKAVKEANAYDFIMKLPHQfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK15056 99 DVVMMG-RYGhmgwlRRAKKRDR--QIVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 126927 556 ATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV 591
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
407-586 |
4.10e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYLreiigvvSQEPVLFAT-TIAE 485
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIKVGYL-------PQEPQLDPTkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 486 NI-------------------RYGREDVTMD-------EIEKAVKEANAYDFIMKLPHQFDTLVGERG----AQLSGGQK 535
Cdd:TIGR03719 88 NVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALRCPPWdadvTKLSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 586
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1054-1259 |
6.10e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1054 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAG------SVFLDGKEIKQLNVQWL---RAHLgiVSQEPILF--- 1121
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGllpgsgSIQFAGQPLEAWSAAELarhRAYL--SQQQTPPFamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 -----DCSIAENIAYGDNSRAVshEEIVRAAKeanihqfidsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVR-----Q 1191
Cdd:PRK03695 86 vfqylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1192 PH--ILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK03695 150 PAgqLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1051-1247 |
6.84e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGSVFLDGKEIKQLnvqwLRAHLGIVSQEPILFDCS-IAE 1127
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----FQRSTGYVEQQDVHSPNLtVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDNSRAVSHEeivraakeanihqfidslpdkyntrvgdkgtqlsggQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:cd03232 99 ALRFSALLRGLSVE------------------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 126927 1208 SEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIENG 1247
Cdd:cd03232 143 AAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
419-609 |
9.22e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.87 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 419 GQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINV---------RYLREIIGVVSQEP-------VLFATT 482
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 483 IAE-----------NIRYGREDvTMDEIEKAVkeanayDFIMKLPHQFdtlvgergaqlSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK11701 112 IGErlmavgarhygDIRATAGD-WLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 552 LLDEATSALDTEseavVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:PRK11701 174 FMDEPTGGLDVS----VQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1060-1241 |
1.60e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.55 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1060 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVfldgkeikqlnvqwlrahlgivsqepILFDCSIAENIAYGDNSravs 1139
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLL---- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1140 heeivraakeanihqfidslpdkyNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-- 1217
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*....
gi 126927 1218 -----KAREGRTCIVIAHRLSTIQNADLI 1241
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1052-1230 |
1.81e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1052 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQL------NVQWLRAHLGIVS----QEPILF 1121
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 DCSIAeniaygdnsRAVSHEEIVRAAKEANIHQFIDsLPDKyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:PRK13538 98 YQRLH---------GPGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 126927 1202 SALDTESEKVVQEALDK-AREGRTCIVIAH 1230
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
122-361 |
3.82e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 65.64 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 122 AGVLIVAYI-QVSLWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:cd18778 43 ALLLLGAYLlRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKEL 273
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 274 ERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTF--SIGHLAPNI 351
Cdd:cd18778 203 KRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSLHGLN 280
|
250
....*....|
gi 126927 352 EAFANARGAA 361
Cdd:cd18778 281 EMLQRALAGA 290
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
758-933 |
3.89e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 65.57 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 758 LVMGLI---SFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVV 834
Cdd:cd18589 40 TVMSLLtiaSAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 835 TQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKF 914
Cdd:cd18589 118 MWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE 197
|
170
....*....|....*....
gi 126927 915 ETMYAQSLQVPYRNAMKKA 933
Cdd:cd18589 198 AQRYRQRLQKTYRLNKKEA 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1049-1249 |
4.37e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVFLD-GKEIKQLNVqwlrahlgIVS---QEP------ 1118
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDL--------IVArlqQDPprnveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILFDcSIAENIA--------YGDNSRAVSHEE----IVRAAK-------------EANIHQFIDSL---PDKyntrvgdK 1170
Cdd:PRK11147 82 TVYD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------A 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1171 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
412-602 |
5.21e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.08 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYlreiigvVSQEPVLFATTIAENIRYgr 491
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLFY-------VPQRPYMTLGTLRDQIIY-- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 492 EDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGA---------QLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:TIGR00954 538 PDSSEDMKRRGLSDKDLEQILDNV--QLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126927 563 ESEavvQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDG 602
Cdd:TIGR00954 616 DVE---GYMYRLCREfGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
374-607 |
5.59e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 374 IDSFSTKGYKPDSIMGN-------LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL 446
Cdd:PRK10522 299 LNKLALAPYKAEFPRPQafpdwqtLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 447 EGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFattiaenirygreDVTMDEIEKAVKEANAYDFI--MKLPHQFdTLVG 524
Cdd:PRK10522 377 SGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-------------DQLLGPEGKPANPALVEKWLerLKMAHKL-ELED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 525 ERGA--QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVV-QAALDKARE-GRTTIVIAHRLSTVRNADVIAGF 600
Cdd:PRK10522 443 GRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEM 522
|
....*..
gi 126927 601 DGGVIVE 607
Cdd:PRK10522 523 RNGQLSE 529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1046-1248 |
5.65e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-QLNVQWLRAHLGIVSQE-PILFDC 1123
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIAYGDNSRA---VSHEEIVRAAKeanihQFIDSLPDKYNTRvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK10982 89 SVMDNMWLGRYPTKgmfVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 1201 TSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIENGK 1248
Cdd:PRK10982 162 TSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
401-583 |
6.09e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 401 PSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIiGVV----SQ-- 474
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 475 --EPVLfattiaENIRYGRE--DVTMDEIEKAVKEanaYDFIMKLPHQFDTLVgeRgaQLSGGQKQRIAIARALVRNPKI 550
Cdd:COG4586 109 wdLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
|
170 180 190
....*....|....*....|....*....|....
gi 126927 551 LLLDEATSALDTESEAVVQAALDKA-REGRTTIV 583
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYnRERGTTIL 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1050-1232 |
6.58e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwLRahLGIVSQEpILFDCSIAENI 1129
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQK-LYLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1130 AYGDNSR-AVSHEEIVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:PRK09544 87 NRFLRLRpGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*.
gi 126927 1209 EKVVQEALDKAREGRTCIV--IAHRL 1232
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1050-1254 |
6.85e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GSVFLDGKEIKQLNVQWL---RAHLGIVSQEP 1118
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1119 ILFdcSIAENIAYG-----DNSRAVSHE--EIVRAAKEanihqfidsLPDKyNTRVGDKGTQLSGGQKQRIAIARAL--- 1188
Cdd:PRK13547 96 FAF--SAREIVLLGryphaRRAGALTHRdgEIAWQALA---------LAGA-TALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1189 ------VRQPHILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1254
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1051-1235 |
8.37e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGiVSQE-----PILFDcSI 1125
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-QSEEvdwsfPVLVE-DV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 AENIAYGDNS---RAVSHE-EIVRAAKEAnihqfIDSLPDKYNtRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:PRK15056 101 VMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|....*
gi 126927 1202 SALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1235
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1049-1239 |
1.01e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1129 IAYG--DNSRAVSHEEIVRAAKEANIHQFIDSLpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:PRK13540 95 CLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....
gi 126927 1207 ESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1239
Cdd:PRK13540 161 LSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
391-595 |
1.01e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIRYG-REDVTMDEIEKAVKeanaydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPK 549
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDiHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126927 550 ILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNAD 595
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1054-1254 |
1.01e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1054 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLR----AHLGIVSQEPI--LFDC 1123
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 -----SIAENI-AYGDNSRAVSHEEIVRAAKEANIhqfidslPDKyNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:PRK11022 106 ytvgfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGI-------PDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1198 DEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGT 1254
Cdd:PRK11022 178 DEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
416-589 |
1.08e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.54 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 416 VKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSiDGQDIRTInVRYLReiiGVVSQEpvLFATTIAENIRYGREDVT 495
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI-LDEFR---GSELQN--YFTKLLEGDVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 496 MDEIEKAVKeANAYDFIMKLP--HQFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:cd03236 96 VDLIPKAVK-GKVGELLKKKDerGKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*.
gi 126927 565 EAVVQAALDK-AREGRTTIVIAHRLS 589
Cdd:cd03236 175 RLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
391-610 |
1.37e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHfnyPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM--QRLYDPLEGVVSIDGQDIRTIN------- 461
Cdd:CHL00131 8 LEIKNLH---ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeerahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 462 -----VRYLREIIGVVSQEpvlFATTIAENIRYGREDVTMDEIEkavkeanAYDFIM-KLPhqfdtLVGERGAQL----- 530
Cdd:CHL00131 85 giflaFQYPIEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLK-----LVGMDPSFLsrnvn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 531 ---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFDGGV 604
Cdd:CHL00131 150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
|
....*.
gi 126927 605 IVEQGN 610
Cdd:CHL00131 230 IIKTGD 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1050-1269 |
1.63e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGSVFLDGKEIKQlnvQWLRaHLGIVSQEPILF-DCSIA 1126
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYGDNSR---AVSHEEIVRAAkEANIHQFidSLPDKYNTRVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PLN03211 159 ETLVFCSLLRlpkSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1203 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLLAqkgiYFSMV 1269
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESV 301
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1049-1261 |
1.71e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.89 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPI----- 1119
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 ----LFDCSIAENIAYGDnsravsHEEIVRAAKEANIHQFIDSL--PDKYNTRVGDKGtqLSGGQKQRIAIARALVRQPH 1193
Cdd:PRK09580 94 snqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1194 ILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIENGKVKEHGTH---QQLLAQ 1261
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
115-342 |
1.87e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 63.27 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 115 YYYTGIGAGVLIVAYIQVSLWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKIND----GIG 186
Cdd:cd18540 42 TGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 187 DkigmFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALwakvltsFTNKELQAYAKAGAVAEEVLAA------- 259
Cdd:cd18540 122 D----LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY-------FQKKILKAYRKVRKINSRITGAfnegitg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 260 IRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFSILL 339
Cdd:cd18540 191 AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIG-TLVAFISYAT 269
|
...
gi 126927 340 GTF 342
Cdd:cd18540 270 QFF 272
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
146-342 |
1.99e-10 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 63.24 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 146 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKIND----GIGDkigmFFQSITTFLAGFIIGFISGWKLTLVILAVS 221
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED----LFISIITIIGSFIILLTINVPLTLIVFALL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 222 PLIGlssalwakVLTSFTNKEL-----QAYAKAG---AVAEEVLAAIRTVIAFGGQQKELERY---NKNLEEAKnvgiKK 290
Cdd:cd18549 153 PLMI--------IFTIYFNKKMkkafrRVREKIGeinAQLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESK----KK 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 126927 291 AITA-SISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF 342
Cdd:cd18549 221 AYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVA--FLLYVNVF 271
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
150-342 |
2.30e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 63.35 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 150 FFHAIMNQEIGWFDVHDVGELNTRLTDdvskiNDGI-----GDKIGMFFQSITTFLAGFIIGFISgWKLTLVILAVSPLI 224
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRFQE-----NQKIrrfltRSALTTILDLLMVFIYLGLMFYYN-LQLTLIVLAFIPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 225 GLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQ----KELERYNKNLeeakNVGIKKAITASISIGI 300
Cdd:cd18568 155 VLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERpirwRWENKFAKAL----NTRFRGQKLSIVLQLI 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 126927 301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTF 342
Cdd:cd18568 231 SSLINHLGTIAVLWYGAYLVISGQLTIGQL--VAFNMLFGSV 270
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
409-610 |
2.49e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 62.63 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPLEG------VVSID----GQDIRTINVR 463
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLhlkkeqpgnHDRIEGlehidkVIVIDqspiGRTPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 YlreiIGVVSQEPVLFATtIAENIRYGRE--DVTM------DEIEKAVKEAnaYDF---IMKLPHQFDTLV--------- 523
Cdd:cd03271 91 Y----TGVFDEIRELFCE-VCKGKRYNREtlEVRYkgksiaDVLDMTVEEA--LEFfenIPKIARKLQTLCdvglgyikl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 524 GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI-- 597
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWIid 243
|
250
....*....|....*..
gi 126927 598 ----AGFDGGVIVEQGN 610
Cdd:cd03271 244 lgpeGGDGGGQVVASGT 260
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
709-869 |
7.93e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 61.37 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrDDDHETKRQNCNLFSLFFLVMGLI-----SFVTYFFQGFTFGKAGEILT 783
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILI-----DDVLIQLGPGGNTSLLLLLVLGLAgayvlSALLGILRGRLLARLGERIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 784 KRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANL-GTGVILsLVYGWQLTLLLVVI 862
Cdd:cd18563 76 ADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIiGIGVVL-FSLNWKLALLVLIP 152
|
....*..
gi 126927 863 IPLIVLG 869
Cdd:cd18563 153 VPLVVWG 159
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
402-611 |
8.41e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqlmqrLYDPLEGVVS---IDGqDIRTINVRYLREIIGVVS----- 473
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTT-------LMDVLAGRKTggyIEG-DIRISGFPKKQETFARISgyceq 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 474 ----------QEPVLFATTIAENIRYGREDVTM--DEIEKAVKEANAYDFIMKLPhqfdtlvGERGaqLSGGQKQRIAIA 541
Cdd:PLN03140 961 ndihspqvtvRESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIA 1031
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 542 RALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGNH 611
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
400-586 |
1.04e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.50 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 400 YPSRSEVQILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI----RTINVRYlreiig 470
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKADY------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 vvsqepvlfattiaenirYGREDVTMDEIEKAVKEANAYDF-IMKlPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPK 549
Cdd:cd03237 75 ------------------EGTVRDLLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDAD 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 126927 550 ILLLDEATSALDTESEAVVQAALDKAREG--RTTIVIAH 586
Cdd:cd03237 136 IYLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
119-342 |
1.23e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 60.99 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 119 GIGAGVLIVAYIQVSLwclAAGRQIHKIRQKFFHAIMNQEIG--------WFDVHDVGELNTRLtDDVSKINDGIGDKIG 190
Cdd:cd18555 45 GIGILILFLLYGLFSF---LRGYIIIKLQTKLDKSLMSDFFEhllklpysFFENRSSGDLLFRA-NSNVYIRQILSNQVI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 191 MFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQ 270
Cdd:cd18555 121 SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 271 KELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF 342
Cdd:cd18555 201 NIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
407-564 |
1.46e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEG-VVSIDGqdirtINVRYLreiigvvSQEPVLFAT-TIA 484
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPG-----IKVGYL-------PQEPQLDPEkTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 485 ENI-------------------RYGREDVTMD-------EIEKAVKEANAYDfimkLPHQF------------DTLVGer 526
Cdd:PRK11819 89 ENVeegvaevkaaldrfneiyaAYAEPDADFDalaaeqgELQEIIDAADAWD----LDSQLeiamdalrcppwDAKVT-- 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 126927 527 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:PRK11819 163 --KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
405-591 |
1.58e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 405 EVQILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLMQRLYDpLEGVVSIDGQDIRTINVRYLREIIGVVSQE---P 476
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEIKKHYRGDVVYNAETDvhfP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 477 VLfatTIAENIRYGREDVT-------MDEIEKAVKEANAYDFIMKLPHQFDTLVGE---RGaqLSGGQKQRIAIARALVR 546
Cdd:TIGR00956 152 HL---TVGETLDFAARCKTpqnrpdgVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLG 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 126927 547 NPKILLLDEATSALDTESeavvqaALDKAREGRTTIVIAHRLSTV 591
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
406-565 |
1.64e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY-LREIIGVVSQE-PVLFATTI 483
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AENI---RYGREDVTMDEiEKAVKEANAYdfimklphqFDTL-----VGERGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10982 91 MDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170
....*....|
gi 126927 556 ATSALdTESE 565
Cdd:PRK10982 161 PTSSL-TEKE 169
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
411-609 |
1.83e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.00 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 411 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--------------RTI-NVRYLREIIGV---- 471
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 472 VSQE--------PVLFATTiaeniRYGREDvtMDEIEKAvkeANAYDFIMKLPhqfdtLVGERGAQLSGGQKQRIAIARA 543
Cdd:PRK11300 103 VAQHqqlktglfSGLLKTP-----AFRRAE--SEALDRA---ATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 544 LVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfdggVIVEQG 609
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1014-1239 |
1.89e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1014 PEIDSYSTeglKPTLLEGNVKF---NG-VQFNyptrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA 1089
Cdd:PRK10938 243 PEPDEPSA---RHALPANEPRIvlnNGvVSYN-----DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1090 GS--VFLDGK---------EIKQlnvqwlraHLGIVSQEPIL---FDCSIAENIAYG--DN---SRAVSHeeivRAAKEA 1150
Cdd:PRK10938 314 YSndLTLFGRrrgsgetiwDIKK--------HIGYVSSSLHLdyrVSTSVRNVILSGffDSigiYQAVSD----RQQKLA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1151 NihQFIDSLpdKYNTRVGDKGTQ-LSGGQkQRIA-IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRT--- 1224
Cdd:PRK10938 382 Q--QWLDIL--GIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqll 456
|
250 260
....*....|....*....|....*.
gi 126927 1225 -----------CivIAHRLSTIQNAD 1239
Cdd:PRK10938 457 fvshhaedapaC--ITHRLEFVPDGD 480
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
120-340 |
2.27e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 60.30 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 120 IGAGVLIVAYIQVSLWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLtDDVSKINDGIGDkigmf 192
Cdd:cd18782 44 IGVVMLVAALLEAVLTALrtylftdTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTG----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 193 fQSITTFL-AGFIIGFIS-----GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAf 266
Cdd:cd18782 118 -TALTTLLdVLFSVIYIAvlfsySPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 267 ggQQKEL-------ERYNKNLEEaknvGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILL 339
Cdd:cd18782 196 --QNAELkarwrwqNRYARSLGE----GFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILS 267
|
.
gi 126927 340 G 340
Cdd:cd18782 268 G 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1054-1205 |
2.29e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1054 LSLEVKKGQTLALVGSSGCGKStvvQLLERFY---DPMAGSVFLDGKEIKQLNVQwLRAHLGIV-----SQEPILF-DCS 1124
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 IAENIAygdnsrAVSHEEI---VRAAKEANI-HQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK15439 358 LAWNVC------ALTHNRRgfwIKPARENAVlERYRRALNIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
....*
gi 126927 1201 TSALD 1205
Cdd:PRK15439 431 TRGVD 435
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1055-1259 |
2.39e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAhlGIV------SQEPILFDCSIAE 1127
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRA--GIMlcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NI---AYGDNSRAVSheeIVRAAKEA-NIHQFIDSLPDKynTRVGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK11288 351 NInisARRHHLRAGC---LINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 1203 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLL 1259
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
395-618 |
2.97e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 395 NVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQrlydPLEGVVSID-GQDIRTINVrylreiigVVS 473
Cdd:PRK11147 5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKST---LMK----ILNGEVLLDdGRIIYEQDL--------IVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 474 ---QEPVLFATT-----IAENI--------RYGR--EDVTMDEIEKAVKE-ANAYDfimKLPH----QFDTLVGERGAQ- 529
Cdd:PRK11147 70 rlqQDPPRNVEGtvydfVAEGIeeqaeylkRYHDisHLVETDPSEKNLNElAKLQE---QLDHhnlwQLENRINEVLAQl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 530 ----------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAHRLSTVRN-ADVIA 598
Cdd:PRK11147 147 gldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIV 224
|
250 260
....*....|....*....|.
gi 126927 599 GFDGGVIVE-QGNHDELMREK 618
Cdd:PRK11147 225 DLDRGKLVSyPGNYDQYLLEK 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
405-609 |
3.19e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLY-DPLEGVVSIDGqdiRTINVRYLREIiGVVSQEPVLFA-T 481
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQgNNFTGTILANN---RKPTKQILKRT-GFVTQDDILYPhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 482 TIAENIRYGREDVTMDEIEKAVKEANAYDFI--MKLPHQFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 557 TSALD-TESEAVVQAALDKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQG 609
Cdd:PLN03211 234 TSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS----RVYQMFDSVLVLSEG 283
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
392-563 |
4.88e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtINVRYL---REI 468
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IgvvsqEPvlfATTIAENIRYGREDVTMDEIEKAVKeanAY--DFIMKlPHQFDTLVgergAQLSGGQKQRIAIARALVR 546
Cdd:PRK11147 394 L-----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLK 457
|
170
....*....|....*..
gi 126927 547 NPKILLLDEATSALDTE 563
Cdd:PRK11147 458 PSNLLILDEPTNDLDVE 474
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
706-969 |
5.91e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 59.03 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 706 WPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQncnLFSLFFLVMGLISFVTYFFQGFTfGKAGEILTKR 785
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTG---FILLYLGLILIQALSVFLFIRLA-GKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 786 VRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIP- 864
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 865 LIVLGGIIEMKLLSGQALKDKKQLEISGKIaTEAIENFRTIVSLTREQK----F----ETMYAQSlqvpyrnaMKKAHVF 936
Cdd:cd18540 155 LAVVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEKnlreFkeltEEMRRAS--------VRAARLS 225
|
250 260 270
....*....|....*....|....*....|...
gi 126927 937 GITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18540 226 ALFLPIVLFLGSIATALVLWYGGILVLAGAITI 258
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
752-968 |
5.93e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 58.65 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18546 40 LAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 832 AVVTQNVANL-GTGVILsLVYGWQLTLLLVVIIPLIVLGGII---EMKLLSGQAlkdkkQLEISGKIAT--EAIENFRTI 905
Cdd:cd18546 118 VQLVVSLLTLvGIAVVL-LVLDPRLALVALAALPPLALATRWfrrRSSRAYRRA-----RERIAAVNADlqETLAGIRVV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 906 VSLTREQKFETMYAQsLQVPYRNAMKKAH-VFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18546 192 QAFRRERRNAERFAE-LSDDYRDARLRAQrLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLT 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
409-584 |
6.10e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY-LREIIGVVS----QEPVLFATTI 483
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AENI------RYGREDVtMDEiEKAVKEANAY--DFIMKLPHQfDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG1129 348 RENItlasldRLSRGGL-LDR-RRERALAEEYikRLRIKTPSP-EQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190
....*....|....*....|....*....|
gi 126927 556 ATSALDTESEAVVQAALDK-AREGRTTIVI 584
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRElAAEGKAVIVI 450
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1049-1263 |
6.42e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFDCSIA-E 1127
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGrE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1128 NIAYGDNSRAVSHEEIVRAA----KEANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126927 1204 LDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:TIGR01257 2101 MDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
751-1003 |
8.31e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 58.23 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 751 NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLaSDASSVKGAmgar 830
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISRF-NDANKIREA---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 831 lavVTQNVANL--------GTGVILsLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGqalKDKKQLEISGKIATEAIENF 902
Cdd:cd18570 115 ---ISSTTISLfldllmviISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPFKK---KNREVMESNAELNSYLIESL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 903 R---TIVSLTREQKFetmyAQSLQVPYRNAMKKAHVFGITF----SFTQAMMYFSYAACFRFGAYLVAQ------QLMTF 969
Cdd:cd18570 188 KgieTIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSnlqsSIKGLISLIGSLLILWIGSYLVIKgqlslgQLIAF 263
|
250 260 270
....*....|....*....|....*....|....
gi 126927 970 eNVMLVFsavVFGAMAagNTSSFAPDYAKAKVSA 1003
Cdd:cd18570 264 -NALLGY---FLGPIE--NLINLQPKIQEAKVAA 291
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1051-1242 |
9.93e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.62 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVqlLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG---IVSQEPI-------- 1119
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIgrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 -----LFD------CSIAENIAYGDNSRAVSH---------EEIVRAAKE-----ANIHQFIDSLPD---KYnTRVGDKG 1171
Cdd:cd03271 89 atytgVFDeirelfCEVCKGKRYNRETLEVRYkgksiadvlDMTVEEALEffeniPKIARKLQTLCDvglGY-IKLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1172 TQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1242
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWII 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1059-1244 |
1.07e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1059 KKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgkeikqlnvqwLRAHLGIVSQEPilfdcSIAENIAY------G 1132
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGE---------------LKPNLGDYDEEP-----SWDEVLKRfrgtelQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1133 DNSRAVSHEEIVRAAKEanihQFIDSLPDKYNTRVGD-------KG-------------------TQLSGGQKQRIAIAR 1186
Cdd:COG1245 150 DYFKKLANGEIKVAHKP----QYVDLIPKVFKGTVREllekvdeRGkldelaeklglenildrdiSELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 1187 ALVRQPHILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1244
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
113-339 |
1.19e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 57.90 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 113 YAYYYTGIGAGVLIVAYIQVSLW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDK 188
Cdd:cd18580 40 YLGVYAALLVLASVLLVLLRWLLfvlaGLRASRRLH---DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 189 IGMFFQSITTFLAGFIIGFISGWkltLVILAVSPLIGLSSALWAKVLTsfTNKELQ---AYAKAGAVA--EEVLAAIRTV 263
Cdd:cd18580 117 LLDFLQSLFSVLGSLIVIAIVSP---YFLIVLPPLLVVYYLLQRYYLR--TSRQLRrleSESRSPLYShfSETLSGLSTI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 264 IAFGGQQKELERYNKNLEEaknvgikkaitasiSIGIAYLLVYASYALAFWYG--TSLVLsneysigeVLTVFFSILL 339
Cdd:cd18580 192 RAFGWQERFIEENLRLLDA--------------SQRAFYLLLAVQRWLGLRLDllGALLA--------LVVALLAVLL 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1048-1261 |
1.33e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRaHLGIV----SQepILFDC 1123
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAENIA-----YGdnsraVSHEEIvraakEANIHQFID--SLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG4586 112 PAIDSFRllkaiYR-----IPDAEY-----KKRLDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1197 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1036-1208 |
1.43e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1036 NGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLlerfydpMAGsvfLD----GKEIKQLNVQwlrahL 1111
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI-------MAG---VDkdfnGEARPQPGIK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1112 GIVSQEPILfDCS--IAENIAYG--------DNSRAVSH-------------------EEIVRAAKEANIHQFIDSLPDK 1162
Cdd:TIGR03719 71 GYLPQEPQL-DPTktVRENVEEGvaeikdalDRFNEISAkyaepdadfdklaaeqaelQEIIDAADAWDLDSQLEIAMDA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126927 1163 YNTRVGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:TIGR03719 150 LRCPPWDaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1033-1256 |
1.63e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPNIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKE----IKQLNVQWLR 1108
Cdd:PLN03073 509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1109 ahlgiVSQEPILFdcsiaeniaygdnsravsHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARAL 1188
Cdd:PLN03073 587 -----LSSNPLLY------------------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAKIT 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1189 VRQPHILLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVIENGKVKE-HGTHQ 1256
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1046-1233 |
1.70e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1046 PNIPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDPMAGSVFLD---GKEIKQLNVQWLRAHLGI- 1113
Cdd:cd03236 12 PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1114 -----VSQEPILFDCSIAENIAYGDNSRAVshEEIVraaKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARAL 1188
Cdd:cd03236 91 vkpqyVDLIPKAVKGKVGELLKKKDERGKL--DELV---DQLELRHVLDRNID-----------QLSGGELQRVAIAAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 1189 VRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLS 1233
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIkqrlNAARLIREL---AEDDNYVLVVEHDLA 200
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
409-614 |
2.32e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 58.87 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPLEG------VVSID----GQDIRTINVR 463
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLngaktvpgrYTSIEGlehldkVIHIDqspiGRTPRSNPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 YlreiIGVVSQEPVLFATT------------IAENIRYGRED---------VTM-------------------------- 496
Cdd:TIGR00630 704 Y----TGVFDEIRELFAETpeakvrgytpgrFSFNVKGGRCEacqgdgvikIEMhflpdvyvpcevckgkrynretlevk 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 497 -------DEIEKAVKEAnaYDFIMKLP---HQFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKILLLD 554
Cdd:TIGR00630 780 ykgkniaDVLDMTVEEA--YEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILD 857
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 555 EATSALDTESEA----VVQAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVEQGNHDEL 614
Cdd:TIGR00630 858 EPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-915 |
2.70e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 57.14 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKG-AMGAR 830
Cdd:cd18564 55 LAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDlLVSGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 831 LAVVTQNVANLGTGVILsLVYGWQLTLLLVVIIPLIVLGgiieMKLLSG---QALKDKKQLEisGKIAT---EAIENFRT 904
Cdd:cd18564 133 LPLLTNLLTLVGMLGVM-FWLDWQLALIALAVAPLLLLA----ARRFSRrikEASREQRRRE--GALASvaqESLSAIRV 205
|
170
....*....|.
gi 126927 905 IVSLTREQKFE 915
Cdd:cd18564 206 VQAFGREEHEE 216
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
194-343 |
4.39e-08 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 56.35 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFL-AGFIIGFIS-----GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFG 267
Cdd:cd18588 118 SALTLVLdLVFSVVFLAvmfyySPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLA 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 268 GQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTFS 343
Cdd:cd18588 198 VEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLAGQVS 271
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
754-988 |
5.14e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 56.05 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 754 SLFFLVMG-----LISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLAsDASSVKGAMG 828
Cdd:cd18566 40 TLQVLVIGvviaiLLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 829 ARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSgQALKDK-KQLEISGKIATEAIENFRTIVS 907
Cdd:cd18566 117 GQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERsRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 908 LTREQ----KFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMyfsyAACFRFGAYLVAQQLMTfenvmlvfsavvFGA 983
Cdd:cd18566 196 MAMEPqmlrRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLVINGDLT------------VGA 259
|
....*
gi 126927 984 MAAGN 988
Cdd:cd18566 260 LIACT 264
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-981 |
5.36e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 56.04 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18565 55 LLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 832 AVVTQNVAN-LGTGVILsLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQL-EISGKIATeAIENFRTIVSLT 909
Cdd:cd18565 133 NSIIRVVVTvLGIGAIL-FYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVgDLNARLEN-NLSGIAVIKAFT 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 910 REQkFET--MYAQSLQvpYRNAMKKAHVFGITFSFT-QAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVF 981
Cdd:cd18565 211 AED-FERerVADASEE--YRDANWRAIRLRAAFFPViRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVGTLVTF 282
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1051-1254 |
5.65e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.11 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGSVFLDGKEIKQLNVQwlrahlgiVSQEP----ILF 1121
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSYKPqyikADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 DCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDS-LPDkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:cd03237 75 EGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDReVPE------------LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1201 TSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVIEnGKVKEHGT 1254
Cdd:cd03237 143 SAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
402-586 |
6.03e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN-VRYlreiIGVVSQEPVLFA 480
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRF----MAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 TTIA-ENIRY-----GREDVTMdeiekavkEANAYDfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:PRK13543 96 DLSTlENLHFlcglhGRRAKQM--------PGSALA-IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 126927 555 EATSALDTESEAVVQAALD-KAREGRTTIVIAH 586
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1049-1260 |
6.54e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHlGIV------SQEPILFD 1122
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1123 CSIAENI---AYGDNSRAVSHeeIVRAAKEANIHQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1200 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLLA 1260
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1147-1242 |
8.64e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.95 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1147 AKEANIHQFIDSLPD---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEK----VVQEAL 1216
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100
....*....|....*....|....*.
gi 126927 1217 DKareGRTCIVIAHRLSTIQNADLIV 1242
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYII 902
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
751-978 |
9.07e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 55.17 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 751 NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGAR 830
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 831 LAVVTQNVANL-GTGVILsLVYGWQLTLLLVVIIPLIVLGgiieMKLLSGQALK-----DKKQLEISGKIAtEAIENFRT 904
Cdd:cd18545 118 LINLIPDLLTLvGIVIIM-FSLNVRLALVTLAVLPLLVLV----VFLLRRRARKawqrvRKKISNLNAYLH-ESISGIRV 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 905 IVSLTRE----QKFETMYAQSLQVpYRNAMKKAHVFGITFSFTQAmmyFSYAACFRFGAYLVAQQLMTFeNVMLVFSA 978
Cdd:cd18545 192 IQSFAREdeneEIFDELNRENRKA-NMRAVRLNALFWPLVELISA---LGTALVYWYGGKLVLGGAITV-GVLVAFIG 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1057-1241 |
1.14e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1057 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDgkeikqLNV----QWLRA-HLGIVSQepilFDCSIAENiaY 1131
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsykpQYIKPdYDGTVED----LLRSITDD--L 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1132 GDNsraVSHEEIVraaKEANIHQFIDSlpdkyntRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:PRK13409 429 GSS---YYKSEII---KPLQLERLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|..
gi 126927 1212 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1241
Cdd:PRK13409 492 VAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1044-1207 |
1.20e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRA-HLGIVSQEPIL-F 1121
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSrFMAYLGHLPGLkA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1122 DCSIAENIAY--GDNSRavsheeivRAAKEANIHQFIDSLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK13543 96 DLSTLENLHFlcGLHGR--------RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*...
gi 126927 1200 ATSALDTE 1207
Cdd:PRK13543 164 PYANLDLE 171
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1055-1261 |
1.26e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS--------VFLDGKEIKQL-NVQWLRAHLGIVSQEPILFDCSI 1125
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1126 AENIAYGdnsravsHEEIVRAAKEANihQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:PRK10938 103 AEIIQDE-------VKDPARCEQLAQ--QFgITALLDR-------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 1205 DTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK10938 167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
755-968 |
1.65e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 54.41 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKG--AMGARLA 832
Cdd:cd18543 43 LLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRflAFGPFLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 833 VvtqNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLeisGKIATEAIEN---FRTIVSLT 909
Cdd:cd18543 121 G---NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQA---GDLATVVEESvtgIRVVKAFG 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 910 RE----QKFETMyAQSLqvpYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18543 195 RErrelDRFEAA-ARRL---RATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLT 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
400-588 |
1.79e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 400 YPSRSEVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPVLf 479
Cdd:TIGR01257 1947 YSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI- 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 480 attiaENIRYGRED---------VTMDEIEKAvkeANAYDFIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPKI 550
Cdd:TIGR01257 2024 -----DDLLTGREHlylyarlrgVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190
....*....|....*....|....*....|....*....
gi 126927 551 LLLDEATSALDTESEAVV-QAALDKAREGRTTIVIAHRL 588
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1058-1271 |
2.22e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1058 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlnvQWlraHLGIVSQEPILFDCSIAENIAYGDNS-R 1136
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGDREyR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1137 AVshEEIVRAAKEAN-------IHQFIDSLpDKYNTR---------VGDKGTQL-------SGGQKQRIAIARALVRQPH 1193
Cdd:PRK10636 93 QL--EAQLHDANERNdghaiatIHGKLDAI-DAWTIRsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1194 ILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHR---LSTIqnADLIVVIENGKVKEH-GTHQQLLAQKGIYFSMV 1269
Cdd:PRK10636 170 LLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISHDrdfLDPI--VDKIIHIEQQSLFEYtGNYSSFEVQRATRLAQQ 245
|
..
gi 126927 1270 QA 1271
Cdd:PRK10636 246 QA 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
391-591 |
2.51e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-PLEGVVSIDGQ--DIRT-------- 459
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNpaqairag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 460 -INVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLvgergAQLSGGQKQRI 538
Cdd:TIGR02633 338 iAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----GRLSGGNQQKA 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126927 539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV 591
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV 466
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1057-1254 |
2.68e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1057 EVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVFLDGKEI-KQLNV----QWL--------RAHLGIVSQEPilFDC 1123
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIsykpQYIspdydgtvEEFLRSANTDD--FGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1124 SIAEniaygdnsravshEEIVRAAKeanihqfIDSLPDKYntrVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:COG1245 433 SYYK-------------TEIIKPLG-------LEKLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1204 LDTESEKVVQEALDKAREGR--TCIVIAHRLSTIqnaDLI---VVIENGKVKEHGT 1254
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIsdrLMVFEGEPGVHGH 538
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
100-340 |
2.74e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 53.74 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 100 IISNSSLEEEMAIyayyytGIGAGVLIVAYI-------QVSLWclaAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELN 171
Cdd:cd18566 32 VIPNESIPTLQVL------VIGVVIAILLESllrllrsYILAW---IGARFdHRLSNAAFEHLLSLPLSFFEREPSGAHL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 172 TRLTDdVSKINDgigdkigmFF--QSITT---------FLAgfIIGFISGWkLTLVILAVSPLIGLSSALWAKVLTSFTN 240
Cdd:cd18566 103 ERLNS-LEQIRE--------FLtgQALLAlldlpfvliFLG--LIWYLGGK-LVLVPLVLLGLFVLVAILLGPILRRALK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 241 KELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLV 320
Cdd:cd18566 171 ERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLV 250
|
250 260
....*....|....*....|
gi 126927 321 LSNEYSIGEVltVFFSILLG 340
Cdd:cd18566 251 INGDLTVGAL--IACTMLSG 268
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1050-1216 |
2.77e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdGKEIK-----QLNVQWLRAhlgivSQEPIlfdcs 1124
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKlgyfaQHQLEFLRA-----DESPL----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1125 iaeniaygdnsravshEEIVRAAKEANIHQFIDSLP------DKyntrVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:PRK10636 396 ----------------QHLARLAPQELEQKLRDYLGgfgfqgDK----VTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170
....*....|....*...
gi 126927 1199 EATSALDTESEKVVQEAL 1216
Cdd:PRK10636 456 EPTNHLDLDMRQALTEAL 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1058-1244 |
2.84e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1058 VKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgkeikqlnvqwLRAHLGIVSQEPilfdcSIAENIAY------ 1131
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGE---------------LIPNLGDYEEEP-----SWDEVLKRfrgtel 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1132 GDNSRAVSHEEIVRAAKEanihQFIDSLPDKYNTRVGD--KGT------------------------QLSGGQKQRIAIA 1185
Cdd:PRK13409 149 QNYFKKLYNGEIKVVHKP----QYVDLIPKVFKGKVREllKKVdergkldevverlglenildrdisELSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1186 RALVRQPHILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1244
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1172-1208 |
2.94e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 2.94e-07
10 20 30
....*....|....*....|....*....|....*..
gi 126927 1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
391-620 |
3.35e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdgqdirTINVRylreiIG 470
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENAN-----IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVL-FATTIA---------------ENIR--YGREDVTMDEIEKAVKeanaydfimklphqfdtlvgergaQLSG 532
Cdd:PRK15064 386 YYAQDHAYdFENDLTlfdwmsqwrqegddeQAVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFDGGVIV 606
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 126927 607 EQGNHDELMREKGI 620
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
118-335 |
3.39e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 53.26 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 118 TGIGAGVLIVAYIQVSLWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSaLWAKVLTSFtnkelqAYAKA-GAVAE------EVLAAIRTVIAF 266
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT-RWFRRRSSR------AYRRArERIAAvnadlqETLAGIRVVQAF 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 267 GGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFF 335
Cdd:cd18546 195 RRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG-VLVAFL 262
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1055-1276 |
5.46e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqLNVQWL---RAHLgivsqEPilfDCSIAENIAY 1131
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1132 GDnsravshEEIVRAAKEANIHQFI-DSL--PDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:PRK11147 407 GK-------QEVMVNGRPRHVLGYLqDFLfhPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1209 EKVVQEALDkAREGrTCIVIAHRLSTIQNAdlivVIE------NGKVKEH-GTHQQLLAQKGIYFSMVQAGAKRS 1276
Cdd:PRK11147 476 LELLEELLD-SYQG-TVLLVSHDRQFVDNT----VTEcwifegNGKIGRYvGGYHDARQQQAQYLALKQPAVKKK 544
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1034-1205 |
6.26e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.49 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1034 KFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGSVFLDGKEIKQLNVQWlRA 1109
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEpilfDCSIAEniaygdnsraVSHEEIVRAAKEANIHQFIdslpdkyntrvgdKGtqLSGGQKQRIAIARALV 1189
Cdd:cd03233 84 EIIYVSEE----DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170
....*....|....*.
gi 126927 1190 RQPHILLLDEATSALD 1205
Cdd:cd03233 135 SRASVLCWDNSTRGLD 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
391-569 |
7.16e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVsidgqdIRTINVRylreiIG 470
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 VVSQEPVLFATTIAENIRYgredvtMDEIEKAVKEanaydfiMKLPHQFDT--LVGERGAQ----LSGGQKQRIAIARAL 544
Cdd:PLN03073 576 VFSQHHVDGLDLSSNPLLY------MMRCFPGVPE-------QKLRAHLGSfgVTGNLALQpmytLSGGQKSRVAFAKIT 642
|
170 180
....*....|....*....|....*.
gi 126927 545 VRNPKILLLDEATSALDTES-EAVVQ 569
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1049-1264 |
7.71e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVfldgkeikqlnvQWL-RAHLGIVSQEP--------I 1119
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1120 LFDCsIAENIAYGDNSRAV---------SHEEIVRAAKeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVR 1190
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1191 QPHILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVIENGKVKEHGTHQQLLAQKGI 1264
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
409-586 |
1.14e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdirtINVRYLREIIGVVSQEPV-LFATT 482
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKPQYIKPDYDGTVeDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 483 IAENIR--YGREDVtmdeIEKavkeanaydfiMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK13409 424 ITDDLGssYYKSEI----IKP-----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180
....*....|....*....|....*...
gi 126927 561 DTESEAVVQAALDKAREGR--TTIVIAH 586
Cdd:PRK13409 485 DVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
114-270 |
1.14e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 51.70 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 114 AYY---YTGIGAGVLIVAYIQVSLWC---LAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGD 187
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFfgsLRASRKLH---ERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 188 KIGMFFQSITTFLAGFIIGFISGWKL---TLVILAVSPLIG---LSSALWAK---------VLTSFTnkelqayakagav 252
Cdd:cd18604 120 SLSSLLESTLSLLVILIAIVVVSPAFllpAVVLAALYVYIGrlyLRASRELKrlesvarspILSHFG------------- 186
|
170
....*....|....*...
gi 126927 253 aeEVLAAIRTVIAFGGQQ 270
Cdd:cd18604 187 --ETLAGLVTIRAFGAEE 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
529-590 |
1.56e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 1.56e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEAVVQAALDKAREGRTTIVIAHRLST 590
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
755-868 |
2.65e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 50.56 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 755 LFFLVMGLI-----SFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGA 829
Cdd:cd18550 38 LVLLALGMVavavaSALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTG 115
|
90 100 110
....*....|....*....|....*....|....*....
gi 126927 830 RLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18550 116 TLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
403-561 |
3.30e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 403 RSEVQILKG-----LNLKVKSGQTVALVGNSGCGKSttvQLMQRLYDPL---EGVVSIDGQDIRTIN--------VRYLR 466
Cdd:PRK10762 257 RLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRT---ELMKVLYGALprtSGYVTLDGHEVVTRSpqdglangIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 E-------IIGV-VSQEPVLFA----TTIAENIRYGREDVTMDeiekavkeanayDFIM----KLPHQfDTLVGErgaqL 530
Cdd:PRK10762 334 EdrkrdglVLGMsVKENMSLTAlryfSRAGGSLKHADEQQAVS------------DFIRlfniKTPSM-EQAIGL----L 396
|
170 180 190
....*....|....*....|....*....|.
gi 126927 531 SGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
138-335 |
3.32e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 50.36 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVI 217
Cdd:cd18561 63 AAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALIL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 218 LAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASIS 297
Cdd:cd18561 143 LVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLS 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 126927 298 IGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFF 335
Cdd:cd18561 223 SGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILF 260
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
391-613 |
3.32e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdGQDIRTINVRYLREIIg 470
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 vvsqEPvlfATTIAENIRYGredvtMDEIEKAVKEAN--AY--DFIMKLPHQfDTLVGergaQLSGGQKQRIAIARALVR 546
Cdd:TIGR03719 398 ----DP---NKTVWEEISGG-----LDIIKLGKREIPsrAYvgRFNFKGSDQ-QKKVG----QLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126927 547 NPKILLLDEATSALDTES-EAVVQAALDKAreGrTTIVIAH-RLSTVRNADVIAGFDGGVIVE--QGNHDE 613
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETlRALEEALLNFA--G-CAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
404-586 |
4.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 404 SEVQILKGLNL-------KVKSGQTVALVGNSGCGKSTTVQLmqrlydpLEGVVSIDGQDIRTINVRYLreiiGVVSQE- 475
Cdd:PRK10636 5 SSLQIRRGVRVlldnataTINPGQKVGLVGKNGCGKSTLLAL-------LKNEISADGGSYTFPGNWQL----AWVNQEt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 476 PVLFATTIAENIRYGREdvtMDEIEKAVKEANAYD---FIMKLPHQFDTL----VGERGAQL------------------ 530
Cdd:PRK10636 74 PALPQPALEYVIDGDRE---YRQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdf 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 586
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
530-609 |
4.98e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 530 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGF 600
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 126927 601 DGGVIVEQG 609
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1155-1242 |
5.32e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.09 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1155 FIDSLPDKYNT-----RVGDKGTQLSGGQKQRIAIARALVRQPH--ILLLDEATSALDTESEKVVQEALDKAR-EGRTCI 1226
Cdd:cd03238 64 FIDQLQFLIDVglgylTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVI 143
|
90
....*....|....*.
gi 126927 1227 VIAHRLSTIQNADLIV 1242
Cdd:cd03238 144 LIEHNLDVLSSADWII 159
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
150-336 |
5.44e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 49.77 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 150 FFHAIMNQEIGWFDVHDVGELNTRLtDDVSKINDGIGDK-IGMFFQSITTFLAGFIIGFISgWKLTLVILAVSPLIGLSS 228
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGfVEALLDGLMAILTLVMMFLYS-PKLALIVLAAVALYALLR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 229 ALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYAS 308
Cdd:cd18567 159 LALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLE 238
|
170 180
....*....|....*....|....*...
gi 126927 309 YALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18567 239 NILVIYLGALLVLDGEFTVG-MLFAFLA 265
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1068-1241 |
5.49e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1068 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAhlgIVSQEPILFDCSIAENIAYGdnSRAVSHEEIVRAA 1147
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY---IGHNLGLKLEMTVFENLKFW--SEIYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1148 keanIHQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-KAREGRTC 1225
Cdd:PRK13541 108 ----IHYFkLHDLLDE-------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIV 176
|
170
....*....|....*.
gi 126927 1226 IVIAHRLSTIQNADLI 1241
Cdd:PRK13541 177 LLSSHLESSIKSAQIL 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
401-633 |
6.48e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 401 PSRSEVQILKG------LNLKVKSGQTVALVGNSGCGKSttvQLMQRLY---DPLEGVVSIDGQdirTINVRYLREII-- 469
Cdd:PRK11288 255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRS---ELMKLLYgatRRTAGQVYLDGK---PIDIRSPRDAIra 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 470 GVV------SQEPVLFATTIAENIRYG--REDVTMDEIEKAVKEA-NAYDFIMKL----PHQfDTLVGergaQLSGGQKQ 536
Cdd:PRK11288 329 GIMlcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQA 483
|
250
....*....|....*....
gi 126927 615 MREKGIyfKLVMTQTRGNE 633
Cdd:PRK11288 484 TERQAL--SLALPRTSAAV 500
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
709-968 |
6.60e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 49.46 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrDDDHETKRQncnLFSLFFLVMGLIsfVTYFFQ-GFTFG------KAGEI 781
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELV-----DLVTIGSKS---LGLLLGLALLLL--GAYLLRaLLNFLriylnhVAEQK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 782 LTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKgamgaRLAV--VTQNVAN----LGTGVILsLVYGWQL 855
Cdd:cd18778 71 VVADLRSDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNvltlVGVAIIL-FSINPKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 856 TLLLVVIIPLIVLGGIIEMKLLSGQAlkdKKQLEISGKIATEAIENF---RTIVSLTREQ----KFETmYAQSLQVPYRN 928
Cdd:cd18778 143 ALLTLIPIPFLALGAWLYSKKVRPRY---RKVREALGELNALLQDNLsgiREIQAFGREEeeakRFEA-LSRRYRKAQLR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 126927 929 AMKKAHVFGITFSFTQAMmyfSYAACFRFGAYLVAQQLMT 968
Cdd:cd18778 219 AMKLWAIFHPLMEFLTSL---GTVLVLGFGGRLVLAGELT 255
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
752-969 |
6.78e-06 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 49.37 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 752 LFSLFFLVMGLISFVTYFfqgftfgkaGEILTKRVRY-M---VFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVkgam 827
Cdd:cd18549 48 LLALYILRTLLNYFVTYW---------GHVMGARIETdMrrdLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 828 gARLA------VVTQNVANLGTGVILSLVYgWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQL-EISGKIaTEAIE 900
Cdd:cd18549 113 -SELAhhgpedLFISIITIIGSFIILLTIN-VPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIgEINAQL-EDSLS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126927 901 NFRTIVSLTRE----QKFETMYAQslqvpYRNAMKKAH-VFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18549 190 GIRVVKAFANEeyeiEKFDEGNDR-----FLESKKKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITL 258
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
408-648 |
8.27e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYlreiigvvsqepvlFATtiaENI 487
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----KGIKLGY--------------FAQ---HQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYGREDVT----MDEIEKAVKEANAYDFIMKLPHQFDTlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK10636 386 EFLRADESplqhLARLAPQELEQKLRDYLGGFGFQGDK-VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 564 -SEAVVQAALDkaREGrTTIVIAHRLSTVRNA--DVIAGFDGGVIVEQGNHDELMRekgIYFKLVMTQTRGNEIEPGNNA 640
Cdd:PRK10636 465 mRQALTEALID--FEG-ALVVVSHDRHLLRSTtdDLYLVHDGKVEPFDGDLEDYQQ---WLSDVQKQENQTDEAPKENNA 538
|
....*...
gi 126927 641 YGSQSDTD 648
Cdd:PRK10636 539 NSAQARKD 546
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
409-586 |
9.25e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLmqrlydpLEGVVSIDGQDIR-TINVRYLREIIGVVSQEPVlfatt 482
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKI-------LAGVLKPDEGEVDeDLKISYKPQYISPDYDGTV----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 483 iaenirygrEDVTMDEIEKAVKEANAYDFIMK---LPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:COG1245 419 ---------EEFLRSANTDDFGSSYYKTEIIKplgLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180
....*....|....*....|....*....
gi 126927 560 LDTESEAVVQAALDKAREGR--TTIVIAH 586
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1044-1251 |
1.07e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GSVFLDGKEIKQLN-VQWLRAHLGIVSQ--- 1116
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSpLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1117 EPILF-DCSIAENIA---------YGDNSRAVSHEEIVRAAKEANihqfiDSLPDKYNTrVGDKGTQLSGGQKQRIAIAR 1186
Cdd:PRK09700 349 DNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 1187 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGKVKE 1251
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1138-1248 |
1.12e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1138 VSHEEivRAAKEANIHQFIDSLPDKYNTRVGD---KGtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvvqe 1214
Cdd:TIGR00956 175 VSREE--YAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT------ 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 126927 1215 ALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIENGK 1248
Cdd:TIGR00956 245 ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
416-588 |
1.48e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 416 VKSGQTVALVGNSGCGKSTTV-----QLMQRLYDPlEGVVSID-------GQDIRTinvrYLREiigvVSQEPVlfatTI 483
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVkilsgELIPNLGDY-EEEPSWDevlkrfrGTELQN----YFKK----LYNGEI----KV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 484 AENIRYgredvtMDEIEKAVKeANAYDFIMKlphqfdtlVGERGA-------------------QLSGGQKQRIAIARAL 544
Cdd:PRK13409 163 VHKPQY------VDLIPKVFK-GKVRELLKK--------VDERGKldevverlglenildrdisELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 126927 545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1033-1234 |
1.65e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.16 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdGKEIKQLNVQWLRAHLg 1112
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1113 ivsqEPilfDCSIAENIAYGdnsravsHEEIVRAAKEANIHQFIDSlpdkYNTRVGD---KGTQLSGGQKQRIAIARALV 1189
Cdd:TIGR03719 398 ----DP---NKTVWEEISGG-------LDIIKLGKREIPSRAYVGR----FNFKGSDqqkKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 126927 1190 RQPHILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1234
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
388-617 |
2.21e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 388 MGNLEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:PRK10938 1 MSSLQISQGTF---RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 468 IigvVSQEpvlFATTIAENIRYGREDV---TMDEIEKAVKEANAydfIMKLPHQF--DTLVGERGAQLSGGQKQRIAIAR 542
Cdd:PRK10938 78 L---VSDE---WQRNNTDMLSPGEDDTgrtTAEIIQDEVKDPAR---CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 543 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1174-1245 |
2.63e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 2.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIE 1245
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
194-349 |
2.87e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 47.54 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 194 QSITTFL-AGFIIGFIsgwkltLVILAVSPLIGL----SSALWAKVLTSF-------TNKELQAYAKAGAVAEEVLAAIR 261
Cdd:cd18779 118 QTLSALLdGTLVLGYL------ALLFAQSPLLGLvvlgLAALQVALLLATrrrvrelMARELAAQAEAQSYLVEALSGIE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 262 TVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvffsilLGT 341
Cdd:cd18779 192 TLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA------LNA 265
|
....*...
gi 126927 342 FSIGHLAP 349
Cdd:cd18779 266 LAGAFLAP 273
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
530-602 |
3.00e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 3.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDG 602
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
391-597 |
5.50e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNypsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTInvrylreiig 470
Cdd:PRK13541 2 LSLHQLQFN----IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 471 vvsQEPvlFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQF--DTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK13541 68 ---AKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 126927 549 KILLLDEATSALDTESEAVVQAALD-KAREGRTTIVIAHRLSTVRNADVI 597
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
402-603 |
6.19e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKS-----TTVQLMQRL----YDP--------LEGVVSID----GQDIRTI 460
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFieqgFCSnlsiqwgaISRLVHITrdlpGRSQRSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 461 NVRY------LREI----------------------IGVVSQEPVLFATTIAEN--------------------IRYGRE 492
Cdd:PRK00635 684 PLTYikafddLRELfaeqprskrlgltkshfsfntpLGACAECQGLGSITTTDNrtsipcpsclgkrflpqvleVRYKGK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 493 DVTmDEIEKAVKEANayDFIMKLPH-----------QFDTL-VGERGAQLSGGQKQRIAIARAL---VRNPKILLLDEAT 557
Cdd:PRK00635 764 NIA-DILEMTAYEAE--KFFLDEPSihekihalcslGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPT 840
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 126927 558 SALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIA--GFDGG 603
Cdd:PRK00635 841 TGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLelGPEGG 889
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
529-600 |
7.69e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 7.69e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 529 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGF 600
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
391-561 |
7.70e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-PLEGVVSIDGQDIRTINVR-YLREI 468
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQqAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 469 IGVVSQE-------PVLfatTIAENI------RYGREDVtmdeIEKAVKEANAYDFIMKL----PHQFdtlvgERGAQLS 531
Cdd:PRK13549 340 IAMVPEDrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLkvktASPE-----LAIARLS 407
|
170 180 190
....*....|....*....|....*....|
gi 126927 532 GGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
409-617 |
8.03e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ-DIRTINVRYLREIIGVvsqepvlfattiaENI 487
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI-------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYgrEDVTMDEIEKAVKEanaydfIMKLPHQFDTLvGERGAQ----LSGGQKQRIAIARALVRNPKILLLDEATSALDte 563
Cdd:PRK13546 107 EF--KMLCMGFKRKEIKA------MTPKIIEFSEL-GEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGD-- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 564 sEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK13546 176 -QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1166-1242 |
9.14e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1166 RVGDKGTQLSGGQKQRIAIARALVRQPH---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1238
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 126927 1239 DLIV 1242
Cdd:PRK00349 900 DWII 903
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1173-1230 |
9.47e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 9.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARegRTCIVIAH 1230
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
405-619 |
9.70e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVqLMQRLYDPLEGVVSIDGQdIRTINVRYLREIIGVvsQEPVLFATTIA 484
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*-TWCANRRALRRTIG*--HRPVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 485 ENiryGREDVTM--DEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:NF000106 101 FS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126927 563 ESE-AVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:NF000106 178 RTRnEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
845-968 |
1.16e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 45.63 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 845 VILSLVYGWQLTLLLVVIIPLIVLggiieMKLLSGQALK--DKKQLEISGKIAT---EAIENFRTIVSLTREQKF----E 915
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPLYVL-----LTLLSSPKLKrnSREIFQANAEQQSflvEALTGIATIKALAAERPIrwrwE 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 126927 916 TMYAQSLQVPYRNAmKKAHVFGITFSFtqaMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18568 208 NKFAKALNTRFRGQ-KLSIVLQLISSL---INHLGTIAVLWYGAYLVISGQLT 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1043-1228 |
1.17e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-MAGSVFLDGKEIKQLNVQWL-----------RA 1109
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1110 HLGIVSQEPILFDCSIAeniaygdNSRAVSHEEIVRAAKEANIHQfidSLPDKYNTR---VGDKGTQLSGGQKQRIAIAR 1186
Cdd:NF040905 348 GYGLNLIDDIKRNITLA-------NLGKVSRRGVIDENEEIKVAE---EYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSK 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 126927 1187 ALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1228
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1168-1263 |
1.29e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1168 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIE 1245
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 126927 1246 NGKVKEHGTHQQLLAQKG 1263
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1051-1261 |
1.30e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikQLNVQWLRAhlGIVSQepilfdCSIAENIA 1130
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAISA--GLSGQ------LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1131 YGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSALDt 1206
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKiiefSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1207 esEKVVQEALDKARE----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
529-586 |
1.32e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 126927 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARegRTTIVIAH 586
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1050-1233 |
1.88e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQLNVQWLRahlGIVSQEPILF-DCSIA 1126
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQETFARIS---GYCEQNDIHSpQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1127 ENIAYGDNSR---AVSHEEIVRAAKEANIHQFIDSLPDKYntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PLN03140 972 ESLIYSAFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAI---VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|..
gi 126927 1203 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLS 1233
Cdd:PLN03140 1049 GLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1051-1263 |
2.22e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgKEIKQLNVQWL------RAHLGIVSQE------- 1117
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGA-----RKIQQGRVEVLggdmadARHRRAVCPRiaympqg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1118 ------PILfdcSIAENIA-----YGdNSRAVSHEEIVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIAR 1186
Cdd:NF033858 85 lgknlyPTL---SVFENLDffgrlFG-QDAAERRRRIDELLRATGLAPFADRPAGK-----------LSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1187 ALVRQPHILLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---DLIVVIENGKVKEHGTHQ 1256
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfDWLVAMDAGRVLATGTPA 222
|
....*..
gi 126927 1257 QLLAQKG 1263
Cdd:NF033858 223 ELLARTG 229
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
530-621 |
2.70e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 530 LSGGQKQRIAIARALVR--NPKIL-LLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VI-----AG 599
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADwIIdlgpeGG 906
|
90 100
....*....|....*....|..
gi 126927 600 FDGGVIVEQGNHDELMREKGIY 621
Cdd:COG0178 907 DGGGEIVAEGTPEEVAKVKASY 928
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
530-595 |
3.12e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 530 LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV------------IAHRLSTVRNAD 595
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1173-1260 |
3.30e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 126927 1250 KEHGTHQQLLA 1260
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
102-286 |
3.87e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 44.06 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 102 SNSSLEEEMAIYAYYYTGIgAGVLIVAYIQVSLW--------CLAAGRQIHKirqKFFHAIMNQEIGWFDVHDVGELNTR 173
Cdd:cd18605 29 SNNSFFNFINDSFNFFLTV-YGFLAGLNSLFTLLraflfaygGLRAARRLHN---KLLSSILFAKMSFFDKTPVGRILNR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 174 LTDDVSKINDGIGDKIGMFFQSITTfLAGFIIGFISGWKLTLVILAVSPLIG----------------LSSALWAKVLTS 237
Cdd:cd18605 105 FSSDVYTIDDSLPFILNILLAQLFG-LLGYLVVICYQLPWLLLLLLPLAFIYyriqryyratsrelkrLNSVNLSPLYTH 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 238 FTnkelqayakagavaeEVLAAIRTVIAFGGQQKELERYNKNLEEAKNV 286
Cdd:cd18605 184 FS---------------ETLKGLVTIRAFRKQERFLKEYLEKLENNQRA 217
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
530-609 |
4.46e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 530 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGF 600
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGV 217
|
....*....
gi 126927 601 DGGVIVEQG 609
Cdd:cd03270 218 HGGEIVAQG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
392-618 |
4.58e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.39 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 392 EFKNVhfnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSttvQLMQRLY--DPL-EGVVSIDGQDIrTINVRY--LR 466
Cdd:PRK09700 267 EVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRaGGEIRLNGKDI-SPRSPLdaVK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 467 EIIGVVSQ---EPVLFAT-TIAENI------RYGREDVTM----DEIEKAVKEANAYDFIMKLpHQFDTLVGErgaqLSG 532
Cdd:PRK09700 338 KGMAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMglfhEVDEQRTAENQRELLALKC-HSVNQNITE----LSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFDGGVIVEQ-G 609
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQIlT 492
|
....*....
gi 126927 610 NHDELMREK 618
Cdd:PRK09700 493 NRDDMSEEE 501
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
391-584 |
5.06e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLMQRLYDP-LEGVVSIDGQDIRTINVR----- 463
Cdd:NF040905 258 FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSdaida 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 464 ---YL---REIIGVVSQEPVLFATTIAENIRYGREDVtMDEIEKaVKEANAY--DFIMKLPHqfdtlVGERGAQLSGGQK 535
Cdd:NF040905 338 glaYVtedRKGYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPS-----VFQKVGNLSGGNQ 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 126927 536 QRIAIARALVRNPKILLLDEATSALDT----ESEAVVQaalDKAREGRTTIVI 584
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIIN---ELAAEGKGVIVI 460
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
752-872 |
5.34e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 43.61 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 752 LFSLFFLVMGLISFVTYFFQGFtfgKAGEILTKRVRYMVFKSMLRqdisWFDdhKNSTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18604 51 LISLLSVLLGTLRYLLFFFGSL---RASRKLHERLLHSVLRAPLR----WLD--TTPVGRILNRFSKDIETIDSELADSL 121
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 126927 832 AVVTQNVANLGTGVILSLVYGWqltLLLVVIIPLIVLGGII 872
Cdd:cd18604 122 SSLLESTLSLLVILIAIVVVSP---AFLLPAVVLAALYVYI 159
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
530-585 |
5.69e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 5.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 126927 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-AVVQAALDKAREGRTTIVIA 585
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
751-968 |
6.54e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.22 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 751 NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFddHKNSTGSLTTRLASdASSVK-----G 825
Cdd:cd18567 42 TVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF--EKRHLGDIVSRFGS-LDEIQqtlttG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 826 AMGARLAVVtqnVAnLGTGVILsLVYGWQLTLLLVVIIPLIVLggiieMKLLSGQALKD--KKQLEISGKIATEAIENFR 903
Cdd:cd18567 119 FVEALLDGL---MA-ILTLVMM-FLYSPKLALIVLAAVALYAL-----LRLALYPPLRRatEEQIVASAKEQSHFLETIR 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126927 904 TIVSL-------TREQKFETMYAQSLqvpyrNAMKKAHVFGITFSFTQAM-MYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18567 189 GIQTIklfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSAANGLlFGLENILVIYLGALLVLDGEFT 256
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
90-279 |
9.53e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 42.98 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 90 TNQSGPNSTLIISNSSLEEEMAIYAYY---YTGIGAGVLIVAYIQ---VSLWCLAAGRQIHkirQKFFHAIMNQEIGWFD 163
Cdd:cd18602 26 TEANHDVASVVFNITSSSLEDDEVSYYisvYAGLSLGAVILSLVTnlaGELAGLRAARRLH---DRMLRNIVRAPMRFFD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 164 VHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFII-GFISGWKLtlviLAVSPLIGLssalwAKVLTSF---T 239
Cdd:cd18602 103 TTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVnAIVTPYFL----IALIPIIIV-----YYFLQKFyraS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126927 240 NKELQ---AYAKAGAVAE--EVLAAIRTVIAFGGQ----QKELERYNKN 279
Cdd:cd18602 174 SRELQrldNITKSPVFSHfsETLGGLTTIRAFRQQarftQQMLELIDRN 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
412-616 |
1.00e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR--------YL---REIIGVVSQEPVLFA 480
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLpedRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 481 T-TIAEN-----IRYGREDVTMDEIEKAVKeanaydfiMKLPHqfdtlvGERGAQ-LSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK15439 362 VcALTHNrrgfwIKPARENAVLERYRRALN--------IKFNH------AEQAARtLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 554 DEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV-----EQGNHDELMR 616
Cdd:PRK15439 428 DEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEISgaltgAAINVDTIMR 497
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
488-621 |
1.02e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 488 RYGRE---------------DVTMDEiekavkeanAYDF---IMKLPHQFDTLV---------GERGAQLSGGQKQRIAI 540
Cdd:PRK00349 771 RYNREtlevkykgkniadvlDMTVEE---------ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKL 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 541 ARALVRNP--KIL-LLDEATSALDTESEA----VVQAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVE 607
Cdd:PRK00349 842 AKELSKRStgKTLyILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDVIKTADWIidlgpeGGDGGGEIVA 918
|
170
....*....|....
gi 126927 608 QGNHDELMREKGIY 621
Cdd:PRK00349 919 TGTPEEVAKVEASY 932
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1172-1242 |
1.06e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1172 TQLSGGQKQRIAIARALVR---QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1242
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
402-597 |
1.15e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 402 SRSEVQILKGLNLkvksgqtvaLVGNSGCGKSTTvqlmqrlydpLEGV-VSIDGQ-DIRTINVRYLREIIGVvsqepvlf 479
Cdd:cd03240 14 ERSEIEFFSPLTL---------IVGQNGAGKTTI----------IEALkYALTGElPPNSKGGAHDPKLIRE-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 480 ATTIAEnIRYGREDVTMDEIeKAVKEANAYDFIMKLPH-QFDTLVGERGAQLSGGQKQ------RIAIARALVRNPKILL 552
Cdd:cd03240 67 GEVRAQ-VKLAFENANGKKY-TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 126927 553 LDEATSALDTESEAVVQAALDKAREG---RTTIVIAHRLSTVRNADVI 597
Cdd:cd03240 145 LDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHI 192
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1173-1242 |
1.36e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126927 1173 QLSGGQKQRIAIARALVRQPH----ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1242
Cdd:cd03227 77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
529-615 |
1.80e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVI 605
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 126927 606 VEQGNHDELM 615
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1046-1081 |
2.01e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 2.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 126927 1046 PNIPV-----LQGLSLEV-----KKGQTLALVGSSGCGKSTVV-QLL 1081
Cdd:PRK01889 170 PGVPVlavsaLDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
707-969 |
3.61e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 41.04 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 707 PYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrqncnLFSLFFLVMGLISFVTYF--FQGFTFGKAGEILTK 784
Cdd:cd18782 2 RALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLAT------LYVIGVVMLVAALLEAVLtaLRTYLFTDTANRIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 785 RVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLaSDASSVKG-AMGARLAVVTQNVANLGTGVILsLVYGWQLTLLLVVII 863
Cdd:cd18782 76 ELGGTIIDHLLRLPLGFFD--KRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIYIAVL-FSYSPLLTLVVLATV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 864 PLIVLggiieMKLLSGQALKD--KKQLEISGKIAT---EAIENFRTIVSLTRE----QKFETMYAQSLQVPYRNAMKKAH 934
Cdd:cd18782 152 PLQLL-----LTFLFGPILRRqiRRRAEASAKTQSylvESLTGIQTVKAQNAElkarWRWQNRYARSLGEGFKLTVLGTT 226
|
250 260 270
....*....|....*....|....*....|....*
gi 126927 935 VFGITFSFTQammyFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18782 227 SGSLSQFLNK----LSSLLVLWVGAYLVLRGELTL 257
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1167-1253 |
5.18e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1167 VGDKGTQLSGGQKQRIAIARALV---RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1242
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90
....*....|.
gi 126927 1243 VIENGKVKEHG 1253
Cdd:PRK00635 1773 EMGPGSGKTGG 1783
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
207-328 |
5.42e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 40.19 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 207 FISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAF---GGQQKE-LERYNKNLEE 282
Cdd:cd18783 137 FFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLalePRQRREwDERVARAIRA 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 126927 283 AKNVGIKKAITASISIGIAYLLVYASyalaFWYGTSLVLSNEYSIG 328
Cdd:cd18783 217 RFAVGRLSNWPQTLTGPLEKLMTVGV----IWVGAYLVFAGSLTVG 258
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1149-1247 |
5.93e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 1149 EANIHQFI--------DSLPdkyntrVGDKGTQLSGGQKQRIAIARAL---VRQPHILLLDEATSALDTESEKVVQEALD 1217
Cdd:PRK00635 783 EPSIHEKIhalcslglDYLP------LGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQ 856
|
90 100 110
....*....|....*....|....*....|.
gi 126927 1218 K-AREGRTCIVIAHRLSTIQNADLivVIENG 1247
Cdd:PRK00635 857 SlTHQGHTVVIIEHNMHVVKVADY--VLELG 885
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
110-226 |
7.16e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 40.15 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 110 MAIYAYYytGIGAGVLIVAY-IQVSLWCLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDK 188
Cdd:cd18606 38 IGIYAGL--GVLQAIFLFLFgLLLAYLGIRASKRLH---NKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDS 112
|
90 100 110
....*....|....*....|....*....|....*...
gi 126927 189 IGMFFQSITTFLAGFIIGFISgwkLTLVILAVSPLIGL 226
Cdd:cd18606 113 LRMFLYTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
533-615 |
7.82e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126927 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH-R--LSTV--RNADViagfDGGVI-V 606
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL-NERNS-TMIIISHdRhfLNSVctHMADL----DYGELrV 232
|
....*....
gi 126927 607 EQGNHDELM 615
Cdd:PRK15064 233 YPGNYDEYM 241
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1174-1242 |
8.14e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 8.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126927 1174 LSGGQKQRIAIARAL------VrqphILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1242
Cdd:cd03270 138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| |
